A species of thermoacidophilic ARCHAEA in the family Sulfolobaceae, found in volcanic areas where the temperature is about 80 degrees C and SULFUR is present.
A species of aerobic, chemolithotrophic ARCHAEA consisting of coccoid cells that utilize sulfur as an energy source. The optimum temperature for growth is 70-75 degrees C. They are isolated from acidic fields.
A family of lemon-shaped DNA viruses infecting ARCHAEA and containing one genus: Fusellovirus.
Deoxyribonucleic acid that makes up the genetic material of archaea.
One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.
Family of rod-shaped DNA viruses infecting ARCHAEA. They lack viral envelopes or lipids.
Structures within the nucleus of archaeal cells consisting of or containing DNA, which carry genetic information essential to the cell.
Viruses whose hosts are in the domain ARCHAEA.
Ribonucleic acid in archaea having regulatory and catalytic roles as well as involvement in protein synthesis.
The functional genetic units of ARCHAEA.
The genetic complement of an archaeal organism (ARCHAEA) as represented in its DNA.
A large group of bacteria including those which oxidize ammonia or nitrite, metabolize sulfur and sulfur compounds, or deposit iron and/or manganese oxides.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
A family of SULFOLOBALES consisting of aerobic or facultatively anaerobic chemolithotrophic cocci, usually occurring singly. They grow best at a pH of about 2.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
An order of CRENARCHAEOTA consisting of aerobic or facultatively aerobic, chemolithotrophic cocci which are extreme thermoacidophiles. They lack peptidoglycan in their cell walls.
A kingdom in the domain ARCHAEA comprised of thermoacidophilic, sulfur-dependent organisms. The two orders are SULFOLOBALES and THERMOPROTEALES.
Repetitive nucleic acid sequences that are principal components of the archaeal and bacterial CRISPR-CAS SYSTEMS, which function as adaptive antiviral defense systems.
A genus of facultatively anaerobic heterotrophic archaea, in the order THERMOPLASMALES, isolated from self-heating coal refuse piles and acid hot springs. They are thermophilic and can grow both with and without sulfur.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
A DNA repair enzyme that catalyzes DNA synthesis during base excision DNA repair. EC 2.7.7.7.
Enzymes that hydrolyze O-glucosyl-compounds. (Enzyme Nomenclature, 1992) EC 3.2.1.-.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
One of the three domains of life (the others being Eukarya and ARCHAEA), also called Eubacteria. They are unicellular prokaryotic microorganisms which generally possess rigid cell walls, multiply by cell division, and exhibit three principal forms: round or coccal, rodlike or bacillary, and spiral or spirochetal. Bacteria can be classified by their response to OXYGEN: aerobic, anaerobic, or facultatively anaerobic; by the mode by which they obtain their energy: chemotrophy (via chemical reaction) or PHOTOTROPHY (via light reaction); for chemotrophs by their source of chemical energy: CHEMOLITHOTROPHY (from inorganic compounds) or chemoorganotrophy (from organic compounds); and by their source for CARBON; NITROGEN; etc.; HETEROTROPHY (from organic sources) or AUTOTROPHY (from CARBON DIOXIDE). They can also be classified by whether or not they stain (based on the structure of their CELL WALLS) with CRYSTAL VIOLET dye: gram-negative or gram-positive.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A class of enzymes that catalyze the hydrolysis of one of the three ester bonds in a phosphotriester-containing compound.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Family of enveloped, lipid-containing, filamentous DNA viruses that infect ARCHAEA.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Protein components of the CRISPR-CAS SYSTEMS for anti-viral defense in ARCHAEA and BACTERIA. These are proteins that carry out a variety of functions during the creation and expansion of the CRISPR ARRAYS, the capture of new CRISPR SPACERS, biogenesis of SMALL INTERFERING RNA (CRISPR or crRNAs), and the targeting and silencing of invading viruses and plasmids. They include DNA HELICASES; RNA-BINDING PROTEINS; ENDONUCLEASES; and RNA and DNA POLYMERASES.
Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
A genus of extremely halophilic HALOBACTERIACEAE which are chemoheterotropic and strictly aerobic. They are found in neutral saline environments such as salt lakes (especially the Dead Sea) and marine salterns.
The rate dynamics in chemical or physical systems.
Cytosine nucleotides which contain deoxyribose as the sugar moiety.
The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Cytochromes (electron-transporting proteins) in which the heme prosthetic group is heme a, i.e., the iron chelate of cytoporphyrin IX. (From Enzyme Nomenclature, 1992, p539)
Proteins prepared by recombinant DNA technology.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
Compounds in which one or more of the three hydroxyl groups of glycerol are in ethereal linkage with a saturated or unsaturated aliphatic alcohol; one or two of the hydroxyl groups of glycerol may be esterified. These compounds have been found in various animal tissue.
A genus of facultatively anaerobic coccoid ARCHAEA, in the family SULFOLOBACEAE. Cells are highly irregular in shape and thermoacidophilic. Lithotrophic growth occurs aerobically via sulfur oxidation in some species. Distribution includes solfataric springs and fields, mudholes, and geothermically heated acidic marine environments.
An enzyme in the tryptophan biosynthetic pathway. EC 4.1.1.48.
A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.
1,4-alpha-D-Glucan-1,4-alpha-D-glucan 4-alpha-D-glucosyltransferase/dextrin 6 alpha-D-glucanohydrolase. An enzyme system having both 4-alpha-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33) activities. As a transferase it transfers a segment of a 1,4-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or another 1,4-alpha-D-glucan. As a glucosidase it catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-1,6-glucosidase activity is deficient in glycogen storage disease type III.
The functional hereditary units of BACTERIA.
A sequence of successive nucleotide triplets that are read as CODONS specifying AMINO ACIDS and begin with an INITIATOR CODON and end with a stop codon (CODON, TERMINATOR).
The large subunit of the archaeal 70s ribosome. It is composed of the 23S RIBOSOMAL RNA, the 5S RIBOSOMAL RNA, and about 40 different RIBOSOMAL PROTEINS.
DNA-dependent DNA polymerases found in bacteria, animal and plant cells. During the replication process, these enzymes catalyze the addition of deoxyribonucleotide residues to the end of a DNA strand in the presence of DNA as template-primer. They also possess exonuclease activity and therefore function in DNA repair.
Enzymes that catalyze a reverse aldol condensation. A molecule containing a hydroxyl group and a carbonyl group is cleaved at a C-C bond to produce two smaller molecules (ALDEHYDES or KETONES). EC 4.1.2.
The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).
The sum of the weight of all the atoms in a molecule.
An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
An oil-resistant synthetic rubber made by the polymerization of chloroprene.
The small subunit of archaeal RIBOSOMES. It is composed of the 16S RIBOSOMAL RNA and about 28 different RIBOSOMAL PROTEINS.
A sulfuric acid dimer, formed by disulfide linkage. This compound has been used to prolong coagulation time and as an antidote in cyanide poisoning.
Adaptive antiviral defense mechanisms, in archaea and bacteria, based on DNA repeat arrays called CLUSTERED REGULARLY INTERSPACED SHORT PALINDROMIC REPEATS (CRISPR elements) that function in conjunction with CRISPR-ASSOCIATED PROTEINS (Cas proteins). Several types have been distinguished, including Type I, Type II, and Type III, based on signature motifs of CRISPR-ASSOCIATED PROTEINS.
The relationships of groups of organisms as reflected by their genetic makeup.
A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A LEUCINE and DNA-binding protein that is found primarily in BACTERIA and ARCHAEA. It regulates GENETIC TRANSCRIPTION involved in METABOLISM of AMINO ACIDS in response to the increased concentration of LEUCINE.
Enzymes that catalyze the exohydrolysis of 1,4-alpha-glucosidic linkages with release of alpha-glucose. Deficiency of alpha-1,4-glucosidase may cause GLYCOGEN STORAGE DISEASE TYPE II.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The process by which a DNA molecule is duplicated.
The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.
Peptide initiation factors from prokaryotic organisms. Only three factors are needed for translation initiation in prokaryotic organisms, which occurs by a far simpler process than in PEPTIDE CHAIN INITIATION, TRANSLATIONAL of eukaryotic organisms.
Enzymes that recognize CRUCIFORM DNA structures and introduce paired incisions that help to resolve the structure into two DNA helices.
Diagnostic aid in pancreas function determination.
An enzyme that catalyzes the transfer of the propylamine moiety from 5'-deoxy-5'-S-(3-methylthiopropylamine)sulfonium adenosine to putrescine in the biosynthesis of spermidine. The enzyme has a molecular weight of approximately 73,000 kDa and is composed of two subunits of equal size.
Orotic acid, also known as pyrophosphoric acid dihydrate, is a organic compound that plays a role in the biosynthesis of pyrimidines, and elevated levels of orotic acid in urine can indicate certain genetic disorders or liver dysfunction.
Dextrins are a group of partially degraded and digestible starches, formed through the hydrolysis of starch by heat, acids, or enzymes, consisting of shorter chain polymers of D-glucose units linked mainly by α-(1→4) and α-(1→6) glycosidic bonds.
The first DNA-binding protein motif to be recognized. Helix-turn-helix motifs were originally identified in bacterial proteins but have since been found in hundreds of DNA-BINDING PROTEINS from both eukaryotes and prokaryotes. They are constructed from two alpha helices connected by a short extended chain of amino acids, which constitute the "turn." The two helices are held at a fixed angle, primarily through interactions between the two helices. (From Alberts et al., Molecular Biology of the Cell, 3d ed, p408-9)
The process by which two molecules of the same chemical composition form a condensation product or polymer.
Constituent of 50S subunit of prokaryotic ribosomes containing about 3200 nucleotides. 23S rRNA is involved in the initiation of polypeptide synthesis.
An order of anaerobic methanogens in the kingdom EURYARCHAEOTA. They are pseudosarcina, coccoid or sheathed rod-shaped and catabolize methyl groups. The cell wall is composed of protein. The order includes one family, METHANOCOCCACEAE. (From Bergey's Manual of Systemic Bacteriology, 1989)
Used in the form of the hydrochloride as a reagent in ANALYTICAL CHEMISTRY TECHNIQUES.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
An important enzyme in the glyoxylic acid cycle which reversibly catalyzes the synthesis of L-malate from acetyl-CoA and glyoxylate. This enzyme was formerly listed as EC 4.1.3.2.
The process of cleaving a chemical compound by the addition of a molecule of water.
The scattering of x-rays by matter, especially crystals, with accompanying variation in intensity due to interference effects. Analysis of the crystal structure of materials is performed by passing x-rays through them and registering the diffraction image of the rays (CRYSTALLOGRAPHY, X-RAY). (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Proteins found in any species of bacterium.
A group of enzymes that catalyze the hydrolysis of diphosphate bonds in compounds such as nucleoside di- and tri-phosphates, and sulfonyl-containing anhydrides such as adenylylsulfate. (Enzyme Nomenclature, 1992) EC 3.6.
D-Glucose:1-oxidoreductases. Catalyzes the oxidation of D-glucose to D-glucono-gamma-lactone and reduced acceptor. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.47; EC 1.1.1.118; EC 1.1.1.119 and EC 1.1.99.10.
A subfamily of HELIX-TURN-HELIX DNA-binding proteins that contain a variable length loop adjacent to the HTH motif. The loop connects two anti-parallel strands and forms a wing when bound to DNA.
A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.
A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)
The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.
Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.
Chemical compounds which yield hydrogen ions or protons when dissolved in water, whose hydrogen can be replaced by metals or basic radicals, or which react with bases to form salts and water (neutralization). An extension of the term includes substances dissolved in media other than water. (Grant & Hackh's Chemical Dictionary, 5th ed)
Specific, characterizable, poisonous chemicals, often PROTEINS, with specific biological properties, including immunogenicity, produced by microbes, higher plants (PLANTS, TOXIC), or ANIMALS.
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
A rigorously mathematical analysis of energy relationships (heat, work, temperature, and equilibrium). It describes systems whose states are determined by thermal parameters, such as temperature, in addition to mechanical and electromagnetic parameters. (From Hawley's Condensed Chemical Dictionary, 12th ed)
Deoxyribonucleic acid that makes up the genetic material of bacteria.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
An exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of GLUCOSE.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
A method for determining the sequence specificity of DNA-binding proteins. DNA footprinting utilizes a DNA damaging agent (either a chemical reagent or a nuclease) which cleaves DNA at every base pair. DNA cleavage is inhibited where the ligand binds to DNA. (from Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
An enzyme that catalyzes the reaction between a purine nucleoside and orthophosphate to form a free purine plus ribose-5-phosphate. EC 2.4.2.1.
The degree of similarity between sequences. Studies of AMINO ACID SEQUENCE HOMOLOGY and NUCLEIC ACID SEQUENCE HOMOLOGY provide useful information about the genetic relatedness of genes, gene products, and species.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A dextrodisaccharide from malt and starch. It is used as a sweetening agent and fermentable intermediate in brewing. (Grant & Hackh's Chemical Dictionary, 5th ed)
Factors that utilize energy from the hydrolysis of GTP to GDP for peptide chain elongation. EC 3.6.1.-.
DNA TOPOISOMERASES that catalyze ATP-independent breakage of one of the two strands of DNA, passage of the unbroken strand through the break, and rejoining of the broken strand. DNA Topoisomerases, Type I enzymes reduce the topological stress in the DNA structure by relaxing the superhelical turns and knotted rings in the DNA helix.
A sequence-specific DNA-binding protein that plays an essential role as a global regulator of yeast cell cycle control. It contains a 56 amino acid MADS-box domain within the N-terminal of the protein and is one of the four founder proteins that structurally define the superfamily of MADS DOMAIN PROTEINS.
Peptide elongation factor 1 is a multisubunit protein that is responsible for the GTP-dependent binding of aminoacyl-tRNAs to eukaryotic ribosomes. The alpha subunit (EF-1alpha) binds aminoacyl-tRNA and transfers it to the ribosome in a process linked to GTP hydrolysis. The beta and delta subunits (EF-1beta, EF-1delta) are involved in exchanging GDP for GTP. The gamma subunit (EF-1gamma) is a structural component.
A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.
A unique DNA sequence of a replicon at which DNA REPLICATION is initiated and proceeds bidirectionally or unidirectionally. It contains the sites where the first separation of the complementary strands occurs, a primer RNA is synthesized, and the switch from primer RNA to DNA synthesis takes place. (Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
A nucleoside consisting of the base guanine and the sugar deoxyribose.
The monomeric units from which DNA or RNA polymers are constructed. They consist of a purine or pyrimidine base, a pentose sugar, and a phosphate group. (From King & Stansfield, A Dictionary of Genetics, 4th ed)
A species of strictly anaerobic, hyperthermophilic archaea which lives in geothermally-heated marine sediments. It exhibits heterotropic growth by fermentation or sulfur respiration.
The spectrometric analysis of fluorescent X-RAYS, i.e. X-rays emitted after bombarding matter with high energy particles such as PROTONS; ELECTRONS; or higher energy X-rays. Identification of ELEMENTS by this technique is based on the specific type of X-rays that are emitted which are characteristic of the specific elements in the material being analyzed. The characteristic X-rays are distinguished and/or quantified by either wavelength dispersive or energy dispersive methods.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
A multisubunit enzyme complex that contains CYTOCHROME B GROUP; CYTOCHROME C1; and iron-sulfur centers. It catalyzes the oxidation of ubiquinol to UBIQUINONE, and transfers the electrons to CYTOCHROME C. In MITOCHONDRIA the redox reaction is coupled to the transport of PROTONS across the inner mitochondrial membrane.
Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.
A genus of anaerobic coccoid METHANOCOCCACEAE whose organisms are motile by means of polar tufts of flagella. These methanogens are found in salt marshes, marine and estuarine sediments, and the intestinal tract of animals.
In bacteria, a group of metabolically related genes, with a common promoter, whose transcription into a single polycistronic MESSENGER RNA is under the control of an OPERATOR REGION.
A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.
The products of chemical reactions that result in the addition of extraneous chemical groups to DNA.

An Lrp-like protein of the hyperthermophilic archaeon Sulfolobus solfataricus which binds to its own promoter. (1/479)

Regulation of gene expression in the domain Archaea, and specifically hyperthermophiles, has been poorly investigated so far. Biochemical experiments and genome sequencing have shown that, despite the prokaryotic cell and genome organization, basal transcriptional elements of members of the domain Archaea (i.e., TATA box-like sequences, RNA polymerase, and transcription factors TBP, TFIIB, and TFIIS) are of the eukaryotic type. However, open reading frames potentially coding for bacterium-type transcription regulation factors have been recognized in different archaeal strains. This finding raises the question of how bacterial and eukaryotic elements interact in regulating gene expression in Archaea. We have identified a gene coding for a bacterium-type transcription factor in the hyperthermophilic archaeon Sulfolobus solfataricus. The protein, named Lrs14, contains a potential helix-turn-helix motif and is related to the Lrp-AsnC family of regulators of gene expression in the class Bacteria. We show that Lrs14, expressed in Escherichia coli, is a highly thermostable DNA-binding protein. Bandshift and DNase I footprint analyses show that Lrs14 specifically binds to multiple sequences in its own promoter and that the region of binding overlaps the TATA box, suggesting that, like the E. coli Lrp, Lrs14 is autoregulated. We also show that the lrs14 transcript is accumulated in the late growth stages of S. solfataricus.  (+info)

Analysis of DNA cleavage by reverse gyrase from Sulfolobus shibatae B12. (2/479)

Reverse gyrase is a type I-5' topoisomerase, which catalyzes a positive DNA supercoiling reaction in vitro. To ascertain how this reaction takes places, we looked at the DNA sequences recognized by reverse gyrase. We used linear DNA fragments of its preferred substrate, the viral SSV1 DNA, which has been shown to be positively supercoiled in vivo. The Sulfolobus shibatae B12 strain, an SSV1 virus host, was chosen for production of reverse gyrase. This naturally occurring system (SSV1 DNA-S. shibatae reverse gyrase) allowed us to determine which SSV1 DNA sequences are bound and cleaved by the enzyme with particularly high selectivity. We show that the presence of ATP decreases the number of cleaved complexes obtained whereas the non-hydrolyzable ATP analog adenosine 5'-[beta, gamma-imido]triphosphate increases it without changing the sequence specificity.  (+info)

The A26G replacement in the consensus sequence A-X-X-X-X-G-K-[T,S] of the guanine nucleotide binding site activates the intrinsic GTPase of the elongation factor 2 from the archaeon Sulfolobus solfataricus. (3/479)

A recombinant form of the elongation factor 2 from the archaeon Sulfolobus solfataricus (SsEF-2), carrying the A26G substitution, has been produced and characterized. The amino acid replacement converted the guanine nucleotide binding consensus sequences A-X-X-X-X-G-K-[T,S] of the elongation factors EF-G or EF-2 into the corresponding G-X-X-X-X-G-K-[T,S] motif which is present in all the other GTP-binding proteins. The rate of poly(U)-directed poly(Phe) synthesis and the ribosome-dependent GTPase activity of A26GSsEF-2 were decreased compared to SsEF-2, thus indicating that the A26G replacement partially affected the function of SsEF-2 during translocation. In contrast, the A26G substitution enhanced the catalytic efficiency of the intrinsic SsEF-2 GTPase triggered by ethylene glycol [Raimo, G., Masullo, M., Scarano, G., & Bocchini, V. (1997) Biochimie 78, 832-837]. Surprisingly, A26GSsEF-2 was able to hydrolyse GTP even in the absence of ethylene glycol; furthermore, the alcohol increased the affinity for GTP without modifying the catalytic constant of A26GSsEF-2 GTPase. Compared to SsEF-2, the affinity of A26GSsEF-2 for [3H]GDP was significantly reduced. These findings suggest that A26 is a regulator of the biochemical functions of SsEF-2. The involvement of this alanine residue in the guanine nucleotide-binding pocket of EF-2 or EF-G is discussed.  (+info)

The interaction between the archaeal elongation factor 1alpha and its nucleotide exchange factor 1beta. (4/479)

In Sulfolobus solfataricus the binding of the exchange factor 1beta (SsEF-1beta) to SsEF-1alpha-GDP displaces the nucleotide and the SsEF-1alpha-SsEF-1beta complex is formed. The complex itself is stable, but it dissociates upon the addition of GDP or Gpp(NH)p but not ATP. Since the rate of the formation of the SsEF-1alpha-SsEF-1beta complex is significatively slower than the rate of the nucleotide exchange catalyzed by SsEF-1beta it can be inferred that in vivo the GDP/GTP exchange reaction proceeds via an SsEF-1alpha-SsEF-1beta interaction without involving the formation of a stable binary complex as an intermediate.  (+info)

Coordinate transcriptional control in the hyperthermophilic archaeon Sulfolobus solfataricus. (5/479)

The existence of a global gene regulatory system in the hyperthermophilic archaeon Sulfolobus solfataricus is described. The system is responsive to carbon source quality and acts at the level of transcription to coordinate synthesis of three physically unlinked glycosyl hydrolases implicated in carbohydrate utilization. The specific activities of three enzymes, an alpha-glucosidase (malA), a beta-glycosidase (lacS), and an alpha-amylase, were reduced 4-, 20-, and 10-fold, respectively, in response to the addition of supplementary carbon sources to a minimal sucrose medium. Western blot analysis using anti-alpha-glucosidase and anti-beta-glycosidase antibodies indicated that reduced enzyme activities resulted exclusively from decreased enzyme levels. Northern blot analysis of malA and lacS mRNAs revealed that changes in enzyme abundance arose primarily from reductions in transcript concentrations. Culture conditions precipitating rapid changes in lacS gene expression were established to determine the response time of the regulatory system in vivo. Full induction occurred within a single generation whereas full repression occurred more slowly, requiring nearly 38 generations. Since lacS mRNA abundance changed much more rapidly in response to a nutrient down shift than to a nutrient up shift, transcript synthesis rather than degradation likely plays a role in the regulatory response.  (+info)

Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein. (6/479)

The archaeon Sulfolobus solfataricus grows optimally at 80 degrees C and pH 2.5 to 3.5 on carbon sources such as yeast extracts, tryptone, and various sugars. Cells rapidly accumulate glucose. This transport activity involves a membrane-bound glucose-binding protein that interacts with its substrate with very high affinity (Kd of 0. 43 microM) and retains high glucose affinity at very low pH values (as low as pH 0.6). The binding protein was extracted with detergent and purified to homogeneity as a 65-kDa glycoprotein. The gene coding for the binding protein was identified in the S. solfataricus P2 genome by means of the amino-terminal amino acid sequence of the purified protein. Sequence analysis suggests that the protein is anchored to the membrane via an amino-terminal transmembrane segment. Neighboring genes encode two membrane proteins and an ATP-binding subunit that are transcribed in the reverse direction, whereas a homologous gene cluster in Pyrococcus horikoshii OT3 was found to be organized in an operon. These data indicate that S. solfataricus utilizes a binding-protein-dependent ATP-binding cassette transporter for the uptake of glucose.  (+info)

Extragenic pleiotropic mutations that repress glycosyl hydrolase expression in the hyperthermophilic archaeon Sulfolobus solfataricus. (7/479)

The hyperthermophilic archaeon Sulfolobus solfataricus employs a catabolite repression-like regulatory system to control enzymes involved in carbon and energy metabolism. To better understand the basis of this system, spontaneous glycosyl hydrolase mutants were isolated using a genetic screen for mutations, which reduced expression of the lacS gene. The specific activities of three glycosyl hydrolases, including an alpha-glucosidase (malA), a beta-glycosidase (lacS), and the major secreted alpha-amylase, were measured in the mutant strains using enzyme activity assays, Western blot analysis, and Northern blot analysis. On the basis of these results the mutants were divided into two classes. Group I mutants exhibited a pleiotropic defect in glycosyl hydrolase expression, while a single group II mutant was altered only in lacS expression. PCR, Southern blot analysis, comparative heterologous expression in Escherichia coli, and DNA sequence analysis excluded cis-acting mutations as the explanation for reduced lacS expression in group I mutants. In contrast lacS and flanking sequences were deleted in the group II mutant. Revertants were isolated from group I mutants using a lacS-specific screen and selection. These revertants were pleiotropic and restored glycosyl hydrolase activity either partially or completely to wild-type levels as indicated by enzyme assays and Western blots. The lacS mutation in the group II mutant, however, was nonrevertible. The existence of group I mutants and their revertants reveals the presence of a trans-acting transcriptional regulatory system for glycosyl hydrolase expression.  (+info)

Control of ribosomal protein L1 synthesis in mesophilic and thermophilic archaea. (8/479)

The mechanisms for the control of ribosomal protein synthesis have been characterized in detail in Eukarya and in Bacteria. In Archaea, only the regulation of the MvaL1 operon (encoding ribosomal proteins MvaL1, MvaL10, and MvaL12) of the mesophilic Methanococcus vannielii has been extensively investigated. As in Bacteria, regulation takes place at the level of translation. The regulator protein MvaL1 binds preferentially to its binding site on the 23S rRNA, and, when in excess, binds to the regulatory target site on its mRNA and thus inhibits translation of all three cistrons of the operon. The regulatory binding site on the mRNA, a structural mimic of the respective binding site on the 23S rRNA, is located within the structural gene about 30 nucleotides downstream of the ATG start codon. MvaL1 blocks a step before or at the formation of the first peptide bond of MvaL1. Here we demonstrate that a similar regulatory mechanism exists in the thermophilic M. thermolithotrophicus and M. jannaschii. The L1 gene is cotranscribed together with the L10 and L11 gene, in all genera of the Euryarchaeota branch of the Archaea studied so far. A potential regulatory L1 binding site located within the structural gene, as in Methanococcus, was found in Methanobacterium thermoautotrophicum and in Pyrococcus horikoshii. In contrast, in Archaeoglobus fulgidus a typical L1 binding site is located in the untranslated leader of the L1 gene as described for the halophilic Archaea. In Sulfolobus, a member of the Crenarchaeota, the L1 gene is part of a long transcript (encoding SecE, NusG, L11, L1, L10, L12). A previously suggested regulatory L1 target site located within the L11 structural gene could not be confirmed as an L1 binding site.  (+info)

"Sulfolobus solfataricus" is not a medical term, but rather a scientific name used in the field of microbiology. It refers to a species of archaea (single-celled microorganisms) that is thermoacidophilic, meaning it thrives in extremely high temperature and acidic environments. This organism is commonly found in volcanic hot springs and solfataras, which are areas with high sulfur content and acidic pH levels.

While not directly related to medical terminology, the study of extremophiles like "Sulfolobus solfataricus" can provide insights into the limits of life and the potential for the existence of microbial life in extreme environments on Earth and potentially on other planets.

"Sulfolobus acidocaldarius" is not a medical term, but a scientific name for a species of archaea (single-celled microorganisms) that is commonly found in extremely acidic and hot environments, such as volcanic hot springs. It is a type of hyperthermophile, meaning it thrives at relatively high temperatures, between 75 to 85°C. The organism is rod-shaped and has a unique cell wall structure that helps protect it from the harsh environmental conditions in which it lives.

While not directly related to human health, Sulfolobus acidocaldarius and other archaea have been studied for their potential applications in biotechnology and industrial processes, such as the production of biofuels and enzymes that can function under extreme conditions.

Fuselloviridae is a family of viruses that infect archaea, particularly members of the order Thermoproteales within the domain Archaea. These viruses are characterized by their unique, lemon-shaped or spindle-shaped (fusiform) morphology and a linear, double-stranded DNA genome with covalently closed hairpin ends. The family Fuselloviridae is part of the order Ligamenvirales, which also includes other archaeal virus families like Lipothrixviridae and Rudiviridae.

Fuselloviruses are known to infect hyperthermophilic archaea, such as Sulfolobus species, living in extreme environments with high temperatures (70-105°C) and low pH values (2-4). The most well-studied member of this family is the Sulfolobus turreted icosahedral virus (STIV), which has a complex virion structure consisting of an icosahedral capsid with protruding turrets at the vertices.

Fuselloviruses have been found to play a role in the horizontal gene transfer among archaea, as they can carry and integrate foreign genes into their host's genome during infection. This ability contributes to the genetic diversity and evolution of archaeal communities in extreme environments.

Archaeal DNA refers to the genetic material present in archaea, a domain of single-celled microorganisms lacking a nucleus. Like bacteria, archaea have a single circular chromosome that contains their genetic information. However, archaeal DNA is significantly different from bacterial and eukaryotic DNA in terms of its structure and composition.

Archaeal DNA is characterized by the presence of unique modifications such as methylation patterns, which help distinguish it from other types of DNA. Additionally, archaea have a distinct set of genes involved in DNA replication, repair, and recombination, many of which are more similar to those found in eukaryotes than bacteria.

One notable feature of archaeal DNA is its resistance to environmental stressors such as extreme temperatures, pH levels, and salt concentrations. This allows archaea to thrive in some of the most inhospitable environments on Earth, including hydrothermal vents, acidic hot springs, and highly saline lakes.

Overall, the study of archaeal DNA has provided valuable insights into the evolutionary history of life on Earth and the unique adaptations that allow these organisms to survive in extreme conditions.

Archaea are a domain of single-celled microorganisms that lack membrane-bound nuclei and other organelles. They are characterized by the unique structure of their cell walls, membranes, and ribosomes. Archaea were originally classified as bacteria, but they differ from bacteria in several key ways, including their genetic material and metabolic processes.

Archaea can be found in a wide range of environments, including some of the most extreme habitats on Earth, such as hot springs, deep-sea vents, and highly saline lakes. Some species of Archaea are able to survive in the absence of oxygen, while others require oxygen to live.

Archaea play important roles in global nutrient cycles, including the nitrogen cycle and the carbon cycle. They are also being studied for their potential role in industrial processes, such as the production of biofuels and the treatment of wastewater.

Rudiviridae is a family of double-stranded, rigid rod-shaped viruses that infect archaea. These viruses have linear genomes and typically measure between 400-700 nanometers in length. They are characterized by their unique tail fibers, which they use to attach to and infect their host cells. Rudiviridae viruses primarily infect hyperthermophilic archaea that live in extreme environments, such as hot springs and deep-sea hydrothermal vents. Due to the limited number of studies on these viruses and their hosts, much is still unknown about their biology and ecological significance.

Archaeal chromosomes refer to the genetic material present in Archaea, a domain of single-celled microorganisms. Like bacteria and eukaryotes, Archaea have their genetic material organized into a single circular chromosome, which is typically smaller than bacterial chromosomes. The archaeal chromosome contains all the genetic information necessary for the organism's survival, including genes coding for proteins, RNA molecules, and regulatory elements that control gene expression.

Archaeal chromosomes are structurally similar to bacterial chromosomes, with a histone-like protein called histone-like protein A (HLP) that helps compact the DNA into a more condensed form. However, archaeal chromosomes also share some features with eukaryotic chromosomes, such as the presence of nucleosome-like structures and the use of similar mechanisms for DNA replication and repair.

Overall, archaeal chromosomes are an important area of study in molecular biology, as they provide insights into the evolution and diversity of life on Earth.

Archaeal viruses are viruses that infect and replicate within archaea, which are single-celled microorganisms without a nucleus. These viruses have unique characteristics that distinguish them from bacterial and eukaryotic viruses. They often possess distinct morphologies, such as icosahedral or filamentous shapes, and their genomes can be composed of double-stranded DNA (dsDNA), single-stranded DNA (ssDNA), double-stranded RNA (dsRNA), or single-stranded RNA (ssRNA).

Archaeal viruses have evolved various strategies to hijack the host cell's machinery for replication, packaging, and release of new virus particles. Some archaeal viruses even encode their own proteins for transcription and translation, suggesting a more complex relationship with their hosts than previously thought. The study of archaeal viruses provides valuable insights into the evolution of viruses and their hosts and has implications for understanding the origins of life on Earth.

Archaeal RNA refers to the Ribonucleic acid (RNA) molecules that are present in archaea, which are a domain of single-celled microorganisms. RNA is a nucleic acid that plays a crucial role in various biological processes, such as protein synthesis, gene expression, and regulation of cellular activities.

Archaeal RNAs can be categorized into different types based on their functions, including:

1. Messenger RNA (mRNA): It carries genetic information from DNA to the ribosome, where it is translated into proteins.
2. Transfer RNA (tRNA): It helps in translating the genetic code present in mRNA into specific amino acids during protein synthesis.
3. Ribosomal RNA (rRNA): It is a structural and functional component of ribosomes, where protein synthesis occurs.
4. Non-coding RNA: These are RNAs that do not code for proteins but have regulatory functions in gene expression and other cellular processes.

Archaeal RNAs share similarities with both bacterial and eukaryotic RNAs, but they also possess unique features that distinguish them from the other two domains of life. For example, archaeal rRNAs contain unique sequence motifs and secondary structures that are not found in bacteria or eukaryotes. These differences suggest that archaeal RNAs have evolved to adapt to the extreme environments where many archaea live.

Overall, understanding the structure, function, and evolution of archaeal RNA is essential for gaining insights into the biology of these unique microorganisms and their roles in various cellular processes.

I'm happy to help! However, I believe there might be a slight mistake in your question. "Archaeal" is not a term used to describe genes but rather a group of single-celled organisms that are classified as archaea.

Archaea are one of the three domains of life, along with bacteria and eukaryotes (which include plants, animals, and fungi). Archaea are unique because they share characteristics with both bacteria and eukaryotes, but they also have many features that are distinctly their own. For example, archaea have a different cell membrane structure than bacteria and eukaryotes, which allows them to thrive in extreme environments such as hot springs, salt mines, and deep-sea vents.

Genes, on the other hand, are segments of DNA that contain the instructions for making proteins or performing other important functions in an organism's cells. All living organisms, including archaea, have genes that are passed down from generation to generation. Archaeal genes are made up of the same four nucleotides (A, T, C, and G) as bacterial and eukaryotic genes, and they code for proteins and RNA molecules that are essential for the survival and reproduction of archaea.

So, to summarize, there is no specific definition for "Archaeal genes" because "archaeal" is not a term used to describe genes. However, we can say that archaeal genes are segments of DNA that contain the instructions for making proteins and performing other important functions in archaea.

An archaeal genome refers to the complete set of genetic material or DNA present in an archaea, a single-celled microorganism that is found in some of the most extreme environments on Earth. The genome of an archaea contains all the information necessary for its survival, including the instructions for building proteins and other essential molecules, as well as the regulatory elements that control gene expression.

Archaeal genomes are typically circular in structure and range in size from about 0.5 to over 5 million base pairs. They contain genes that are similar to those found in bacteria and eukaryotes, as well as unique genes that are specific to archaea. The study of archaeal genomes has provided valuable insights into the evolutionary history of life on Earth and has helped scientists understand the adaptations that allow these organisms to thrive in such harsh environments.

Gram-negative chemolithotrophic bacteria are a type of bacteria that obtain energy by oxidizing inorganic substances, such as nitrogen, sulfur, or iron compounds, in a process called chemolithotrophy. They are classified as gram-negative because they do not retain the crystal violet stain used in the Gram staining method, which is a technique used to classify bacteria based on their cell wall structure.

Gram-negative bacteria have a thin peptidoglycan layer and an outer membrane containing lipopolysaccharides (LPS), which make them more resistant to certain antibiotics and chemical agents. The term "chemolithotrophic" refers to their ability to use inorganic chemicals as a source of energy, and they are often found in environments with high concentrations of these substances, such as soil, water, and waste treatment facilities.

Examples of gram-negative chemolithotrophic bacteria include species of the genera Nitrosomonas, Nitrobacter, Thiobacillus, and Sulfurimonas, among others. These bacteria play important roles in the global nitrogen and sulfur cycles, contributing to the oxidation of ammonia to nitrite (Nitrosomonas) or nitrite to nitrate (Nitrobacter), and the oxidation of sulfide or elemental sulfur to sulfuric acid (Thiobacillus).

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

In a medical context, "hot temperature" is not a standard medical term with a specific definition. However, it is often used in relation to fever, which is a common symptom of illness. A fever is typically defined as a body temperature that is higher than normal, usually above 38°C (100.4°F) for adults and above 37.5-38°C (99.5-101.3°F) for children, depending on the source.

Therefore, when a medical professional talks about "hot temperature," they may be referring to a body temperature that is higher than normal due to fever or other causes. It's important to note that a high environmental temperature can also contribute to an elevated body temperature, so it's essential to consider both the body temperature and the environmental temperature when assessing a patient's condition.

Enzyme stability refers to the ability of an enzyme to maintain its structure and function under various environmental conditions, such as temperature, pH, and the presence of denaturants or inhibitors. A stable enzyme retains its activity and conformation over time and across a range of conditions, making it more suitable for industrial and therapeutic applications.

Enzymes can be stabilized through various methods, including chemical modification, immobilization, and protein engineering. Understanding the factors that affect enzyme stability is crucial for optimizing their use in biotechnology, medicine, and research.

Sulfolobaceae is a family of archaea within the order Sulfolobales. These are thermophilic and acidophilic organisms, meaning they thrive in high temperature and low pH conditions. They are commonly found in volcanic hot springs and other extreme environments. Members of this family obtain energy through the oxidation of sulfur compounds and are therefore also called sulfur-oxidizing archaea. The type genus of this family is Sulfolobus.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Sulfolobales is not a medical term, but a taxonomic category in the field of microbiology. It refers to an order of extremophilic archaea, which are single-celled organisms that lack a nucleus and other membrane-bound organelles.

Members of Sulfolobales are characterized by their ability to thrive in harsh environments with high temperatures (often above 80°C) and acidic pH levels (typically below 4). They are commonly found in volcanic hot springs, sulfur-rich mudpots, and other geothermal areas.

The order Sulfolobales includes several genera of archaea, such as Sulfolobus, Acidianus, and Metallosphaera, among others. These organisms have attracted scientific interest due to their unique metabolic pathways and potential applications in biotechnology.

Crenarchaeota is a phylum within the domain Archaea. Members of this group are typically extremophiles, living in harsh environments such as hot springs, deep-sea hydrothermal vents, and highly acidic or alkaline habitats. They are characterized by their unique archaeal-type rRNA genes and distinct cell wall composition. Some Crenarchaeota have been found to be involved in nitrogen and carbon cycling in various environments, including the ocean and soil. However, much is still unknown about this group due to the difficulty of culturing many of its members in the lab.

Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR) is a bacterial defense system that confers resistance to foreign genetic elements such as plasmids and phages, by incorporating short sequences of the invasive genetic material into their own genome. These sequences are then used to recognize and destroy subsequent invasions by identical or similar genetic elements. The CRISPR system consists of two main components: the CRISPR array, which contains the repeats and spacers, and the Cas (CRISPR-associated) proteins, which provide the enzymatic activity for interference.

The CRISPR array is a stretch of DNA in the bacterial genome that contains repetitive sequences interspaced with unique sequences known as "spacers". The repeats are typically palindromic, meaning they read the same backwards as forwards, and are usually 24-48 base pairs long. The spacers are derived from the genetic material of previous invasions by viruses or plasmids, and are used to recognize and target similar sequences in future invaders.

The Cas proteins associated with the CRISPR array provide the enzymatic activity for interference. They can be classified into several different types based on their sequence and domain organization. The most well-studied type is Cas9, which uses a guide RNA derived from the CRISPR array to recognize and cleave specific sequences in the target DNA. This system has been harnessed as a powerful tool for genome editing in various organisms, including humans.

In summary, Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR) is a bacterial defense system that confers resistance to foreign genetic elements by incorporating short sequences of the invasive genetic material into their own genome and using them to recognize and destroy subsequent invasions by identical or similar genetic elements. The CRISPR system consists of two main components: the CRISPR array, which contains the repeats and spacers, and the Cas (CRISPR-associated) proteins, which provide the enzymatic activity for interference.

Thermoplasma is a genus of archaea, which are single-celled microorganisms that lack a nucleus and other membrane-bound organelles. Thermoplasma species are extremophiles, meaning they thrive in extreme environments that are hostile to most other life forms. Specifically, Thermoplasma species are thermoacidophiles, which means they grow optimally at relatively high temperatures (45-60°C) and low pH levels (around 2).

Thermoplasma species have an unusual way of dealing with the harsh conditions of their environment. They lack a cell wall, which makes them highly resistant to heat and acidity. Instead, they have a unique outer membrane that is composed of proteins and lipids, which provides stability and protection in extreme environments.

Thermoplasma species are found in various habitats, including self-heating coal refuse piles, sulfur-rich hot springs, and solfataric fields. They have also been isolated from the acidic environments of industrial waste sites and even from the human mouth. Thermoplasma species are important in biotechnology due to their ability to produce enzymes that can function under extreme conditions, making them useful for various industrial applications.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Temperature, in a medical context, is a measure of the degree of hotness or coldness of a body or environment. It is usually measured using a thermometer and reported in degrees Celsius (°C), degrees Fahrenheit (°F), or kelvin (K). In the human body, normal core temperature ranges from about 36.5-37.5°C (97.7-99.5°F) when measured rectally, and can vary slightly depending on factors such as time of day, physical activity, and menstrual cycle. Elevated body temperature is a common sign of infection or inflammation, while abnormally low body temperature can indicate hypothermia or other medical conditions.

DNA polymerase beta is a type of enzyme that plays a crucial role in the repair and maintenance of DNA in cells. It is a member of the DNA polymerase family, which are enzymes responsible for synthesizing new strands of DNA during replication and repair processes.

More specifically, DNA polymerase beta is involved in the base excision repair (BER) pathway, which is a mechanism for correcting damaged or mismatched bases in DNA. This enzyme functions by removing the damaged or incorrect base and replacing it with a new, correct one, using the undamaged strand as a template.

DNA polymerase beta has several key features that make it well-suited to its role in BER. It is highly processive, meaning that it can add many nucleotides to the growing DNA chain before dissociating from the template. It also has a high catalytic rate and is able to efficiently incorporate new nucleotides into the DNA chain.

Overall, DNA polymerase beta is an essential enzyme for maintaining genomic stability and preventing the accumulation of mutations in cells. Defects in this enzyme have been linked to various human diseases, including cancer and neurodegenerative disorders.

Glucosidases are a group of enzymes that catalyze the hydrolysis of glycosidic bonds, specifically at the non-reducing end of an oligo- or poly saccharide, releasing a single sugar molecule, such as glucose. They play important roles in various biological processes, including digestion of carbohydrates and the breakdown of complex glycans in glycoproteins and glycolipids.

In the context of digestion, glucosidases are produced by the pancreas and intestinal brush border cells to help break down dietary polysaccharides (e.g., starch) into monosaccharides (glucose), which can then be absorbed by the body for energy production or storage.

There are several types of glucosidases, including:

1. α-Glucosidase: This enzyme is responsible for cleaving α-(1→4) and α-(1→6) glycosidic bonds in oligosaccharides and disaccharides, such as maltose, maltotriose, and isomaltose.
2. β-Glucosidase: This enzyme hydrolyzes β-(1→4) glycosidic bonds in cellobiose and other oligosaccharides derived from plant cell walls.
3. Lactase (β-Galactosidase): Although not a glucosidase itself, lactase is often included in this group because it hydrolyzes the β-(1→4) glycosidic bond between glucose and galactose in lactose, yielding free glucose and galactose.

Deficiencies or inhibition of these enzymes can lead to various medical conditions, such as congenital sucrase-isomaltase deficiency (an α-glucosidase deficiency), lactose intolerance (a lactase deficiency), and Gaucher's disease (a β-glucocerebrosidase deficiency).

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Bacteria are single-celled microorganisms that are among the earliest known life forms on Earth. They are typically characterized as having a cell wall and no membrane-bound organelles. The majority of bacteria have a prokaryotic organization, meaning they lack a nucleus and other membrane-bound organelles.

Bacteria exist in diverse environments and can be found in every habitat on Earth, including soil, water, and the bodies of plants and animals. Some bacteria are beneficial to their hosts, while others can cause disease. Beneficial bacteria play important roles in processes such as digestion, nitrogen fixation, and biogeochemical cycling.

Bacteria reproduce asexually through binary fission or budding, and some species can also exchange genetic material through conjugation. They have a wide range of metabolic capabilities, with many using organic compounds as their source of energy, while others are capable of photosynthesis or chemosynthesis.

Bacteria are highly adaptable and can evolve rapidly in response to environmental changes. This has led to the development of antibiotic resistance in some species, which poses a significant public health challenge. Understanding the biology and behavior of bacteria is essential for developing strategies to prevent and treat bacterial infections and diseases.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Phosphoric triester hydrolases are a class of enzymes that catalyze the hydrolysis of phosphoric triesters into corresponding alcohols and phosphates. These enzymes play a crucial role in the detoxification of organophosphate pesticides and nerve agents, as well as in the metabolism of various endogenous compounds.

The term "phosphoric triester hydrolases" is often used interchangeably with "phosphotriesterases" or "organophosphorus hydrolases." These enzymes are characterized by their ability to cleave the P-O-C bond in phosphoric triesters, releasing a free alcohol and a diethyl phosphate moiety.

Phosphoric triester hydrolases have attracted significant interest due to their potential applications in bioremediation, biosensors, and therapeutics. However, it is important to note that the specificity and efficiency of these enzymes can vary widely depending on the structure and properties of the target compounds.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Glucose 1-Dehydrogenase (G1DH) is an enzyme that catalyzes the oxidation of β-D-glucose into D-glucono-1,5-lactone and reduces the cofactor NAD+ into NADH. This reaction plays a role in various biological processes, including glucose sensing and detoxification of reactive carbonyl species. G1DH is found in many organisms, including humans, and has several isoforms with different properties and functions.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Lipothrixviridae is a family of enveloped, rod-shaped viruses that infect archaea. These viruses have a unique lipid membrane derived from the host cell and a linear, double-stranded DNA genome. The virions are typically long and thin, with a hollow core and helical symmetry. Lipothrixviridae is named after its characteristic lipid membrane and rigid structure.

The family Lipothrixviridae includes only one genus, Thermopolisibacteriovirus, which contains several species of viruses that infect thermophilic archaea in the order Crenarchaeota. The prototypical member of this family is the virus SIRV2 (Sulfolobus islandicus rod-shaped virus 2).

Lipothrixviridae viruses have a complex life cycle, involving attachment to the host cell surface, membrane fusion, and injection of the viral genome into the host cytoplasm. The viral DNA is then replicated using the host's replication machinery, and new virions are assembled in the host cell before being released by lysis or extrusion.

Infection with Lipothrixviridae viruses can have significant impacts on the host archaea, including alterations to their metabolism, growth rate, and morphology. However, the precise mechanisms of these effects are not well understood and require further study.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

CRISPR-associated proteins, often abbreviated as Cas proteins, are a type of enzyme that are involved in the CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) immune system found in bacteria and archaea. The CRISPR-Cas system provides adaptive immunity to these single-celled organisms by providing protection against foreign genetic elements, such as viruses and plasmids.

The Cas proteins play a crucial role in the CRISPR-Cas system by cleaving invading nucleic acids at specific sequences, guided by small RNA molecules known as CRISPR RNAs (crRNAs). These crRNAs are derived from short sequences of DNA that are integrated into the CRISPR array during a previous infection. The Cas proteins use these crRNAs to recognize and cleave complementary sequences in the invading nucleic acids, thereby providing immunity against future infections by the same genetic element.

There are several different types of CRISPR-Cas systems, each with their own distinct set of Cas proteins and mechanisms for target recognition and cleavage. The most well-known and widely used CRISPR-Cas system is Type II, which includes the Cas9 protein. This system has been adapted for use in a variety of genome editing applications, including gene therapy, crop modification, and basic research.

Ferredoxins are iron-sulfur proteins that play a crucial role in electron transfer reactions in various biological systems, particularly in photosynthesis and nitrogen fixation. They contain one or more clusters of iron and sulfur atoms (known as the iron-sulfur cluster) that facilitate the movement of electrons between different molecules during metabolic processes.

Ferredoxins have a relatively simple structure, consisting of a polypeptide chain that binds to the iron-sulfur cluster. This simple structure allows ferredoxins to participate in a wide range of redox reactions and makes them versatile electron carriers in biological systems. They can accept electrons from various donors and transfer them to different acceptors, depending on the needs of the cell.

In photosynthesis, ferredoxins play a critical role in the light-dependent reactions by accepting electrons from photosystem I and transferring them to NADP+, forming NADPH. This reduced form of nicotinamide adenine dinucleotide phosphate (NADPH) is then used in the Calvin cycle for carbon fixation and the production of glucose.

In nitrogen fixation, ferredoxins help transfer electrons to the nitrogenase enzyme complex, which reduces atmospheric nitrogen gas (N2) into ammonia (NH3), making it available for assimilation by plants and other organisms.

Overall, ferredoxins are essential components of many metabolic pathways, facilitating electron transfer and energy conversion in various biological systems.

"Haloferax" is a genus of halophilic archaea, which are organisms that thrive in highly saline environments. Members of this genus are typically found in salt lakes, salt pans, and other hypersaline habitats. They are characterized by their ability to grow optimally at sodium chloride concentrations of around 2-3 M (10-15% w/v), which is roughly ten times the salinity of seawater.

The name "Haloferax" comes from the Greek words "halos," meaning salt, and "phorax," meaning carrier or bearer, reflecting their ability to thrive in high-salt environments. These archaea are known for their versatility in terms of energy metabolism, as they can grow either aerobically or anaerobically using various electron donors and acceptors. They also play a significant role in the global nitrogen cycle, as some species are capable of denitrification and nitrate reduction.

It is important to note that "Haloferax" is not a medical term per se but rather a taxonomic designation for a group of archaea with specific ecological and physiological characteristics. However, understanding the biology and ecology of these organisms can contribute to our broader knowledge of microbial diversity, evolution, and adaptation to extreme environments.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Deoxycytosine nucleotides are chemical compounds that are the building blocks of DNA, one of the two nucleic acids found in cells. Specifically, deoxycytosine nucleotides consist of a deoxyribose sugar, a phosphate group, and the nitrogenous base cytosine.

In DNA, deoxycytosine nucleotides pair with deoxyguanosine nucleotides through hydrogen bonding between the bases to form a stable structure that stores genetic information. The synthesis of deoxycytosine nucleotides is tightly regulated in cells to ensure proper replication and repair of DNA.

Disruptions in the regulation of deoxycytosine nucleotide metabolism can lead to various genetic disorders, including mitochondrial DNA depletion syndromes and cancer. Therefore, understanding the biochemistry and regulation of deoxycytosine nucleotides is crucial for developing effective therapies for these conditions.

Crystallization is a process in which a substance transitions from a liquid or dissolved state to a solid state, forming a crystal lattice. In the medical context, crystallization can refer to the formation of crystals within the body, which can occur under certain conditions such as changes in pH, temperature, or concentration of solutes. These crystals can deposit in various tissues and organs, leading to the formation of crystal-induced diseases or disorders.

For example, in patients with gout, uric acid crystals can accumulate in joints, causing inflammation, pain, and swelling. Similarly, in nephrolithiasis (kidney stones), minerals in the urine can crystallize and form stones that can obstruct the urinary tract. Crystallization can also occur in other medical contexts, such as in the formation of dental calculus or plaque, and in the development of cataracts in the eye.

Cytochrome a is a type of cytochrome found in the inner mitochondrial membrane of eukaryotic cells. It is a component of cytochrome c oxidase, the final enzyme in the electron transport chain responsible for reducing molecular oxygen to water during cellular respiration. Cytochrome a contains a heme group with a low redox potential, making it capable of accepting electrons from cytochrome c and transferring them to oxygen.

The "Cytochrome a Group" typically refers to a family of related cytochromes that share similar structural and functional properties, including the presence of a heme group with a low redox potential. This group includes cytochrome a, as well as other closely related cytochromes such as cytochrome aa3 and cytochrome o. These cytochromes play important roles in electron transfer and energy conservation during cellular respiration in various organisms.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which remains unchanged at the end of the reaction. A catalyst lowers the activation energy required for the reaction to occur, thereby allowing the reaction to proceed more quickly and efficiently. This can be particularly important in biological systems, where enzymes act as catalysts to speed up metabolic reactions that are essential for life.

Glyceryl ethers, also known as glycerol ethers or alkyl glycosides, are a class of compounds formed by the reaction between glycerol and alcohols. In the context of medical definitions, glyceryl ethers may refer to a group of naturally occurring compounds found in some organisms, including humans.

These compounds are characterized by an ether linkage between the glycerol molecule and one or more alkyl chains, which can vary in length. Glyceryl ethers have been identified as components of various biological tissues, such as lipid fractions of human blood and lung surfactant.

In some cases, glyceryl ethers may also be used as pharmaceutical excipients or drug delivery systems due to their unique physicochemical properties. For example, they can enhance the solubility and bioavailability of certain drugs, making them useful in formulation development. However, it is important to note that specific medical applications and uses of glyceryl ethers may vary depending on the particular compound and its properties.

'Acidianus' is a genus of thermoacidophilic archaea, which are extremophiles that thrive in extremely acidic and hot environments. These microorganisms are commonly found in volcanic areas, such as sulfur-rich hot springs and deep-sea hydrothermal vents, where the pH levels can be as low as 0 and the temperature can reach up to 90°C (194°F).

The name 'Acidianus' is derived from the Latin word "acidus," meaning sour or acidic, and the Greek word "ianos," meaning belonging to. Therefore, the medical definition of 'Acidianus' refers to a genus of archaea that are adapted to survive in highly acidic environments.

These microorganisms have developed unique metabolic pathways to generate energy from sulfur compounds and other reduced substances present in their environment. They play an essential role in the global carbon and sulfur cycles, contributing to the breakdown of organic matter and the formation of elemental sulfur and sulfate.

Understanding the biology and ecology of 'Acidianus' and other thermoacidophilic archaea can provide insights into the limits of life on Earth and help us explore the potential for extraterrestrial life in extreme environments, such as those found on Mars or other planets.

Indole-3-glycerol-phosphate synthase (IGPS) is an enzyme that catalyzes the conversion of tryptophan into indole-3-glycerol phosphate, which is a key intermediate in the biosynthesis of various physiologically important compounds such as auxins (a type of plant hormone). In humans, defects in the IGPS enzyme have been associated with the disorder phenylketonuria (PKU), which is characterized by an inability to metabolize the amino acid phenylalanine. However, it's worth noting that IGPS primarily functions in the context of plant and microbial metabolism.

Iron-sulfur proteins are a group of metalloproteins that contain iron and sulfur atoms in their active centers. These clusters of iron and sulfur atoms, also known as iron-sulfur clusters, can exist in various forms, including Fe-S, 2Fe-2S, 3Fe-4S, and 4Fe-4S structures. The iron atoms are coordinated to the protein through cysteine residues, while the sulfur atoms can be in the form of sulfide (S2-) or sulfane (-S-).

These proteins play crucial roles in many biological processes, such as electron transfer, redox reactions, and enzyme catalysis. They are found in various organisms, from bacteria to humans, and are involved in a wide range of cellular functions, including energy metabolism, photosynthesis, nitrogen fixation, and DNA repair.

Iron-sulfur proteins can be classified into several categories based on their structure and function, such as ferredoxins, Rieske proteins, high-potential iron-sulfur proteins (HiPIPs), and radical SAM enzymes. Dysregulation or mutations in iron-sulfur protein genes have been linked to various human diseases, including neurodegenerative disorders, cancer, and mitochondrial disorders.

The Glycogen Debranching Enzyme System, also known as glycogen debranching enzyme or Amy-1, is a crucial enzyme complex in human biochemistry. It plays an essential role in the metabolism of glycogen, which is a large, branched polymer of glucose that serves as the primary form of energy storage in animals and fungi.

The Glycogen Debranching Enzyme System consists of two enzymatic activities: a transferase and an exo-glucosidase. The transferase activity transfers a segment of a branched glucose chain to another part of the same or another glycogen molecule, while the exo-glucosidase activity cleaves the remaining single glucose units from the outer branches of the glycogen molecule.

This enzyme system is responsible for removing the branched structures of glycogen, allowing the linear chains to be further degraded by other enzymes into glucose molecules that can be used for energy production or stored for later use. Defects in this enzyme complex can lead to several genetic disorders, such as Glycogen Storage Disease Type III (Cori's disease) and Type IV (Andersen's disease), which are characterized by the accumulation of abnormal glycogen molecules in various tissues.

A bacterial gene is a segment of DNA (or RNA in some viruses) that contains the genetic information necessary for the synthesis of a functional bacterial protein or RNA molecule. These genes are responsible for encoding various characteristics and functions of bacteria such as metabolism, reproduction, and resistance to antibiotics. They can be transmitted between bacteria through horizontal gene transfer mechanisms like conjugation, transformation, and transduction. Bacterial genes are often organized into operons, which are clusters of genes that are transcribed together as a single mRNA molecule.

It's important to note that the term "bacterial gene" is used to describe genetic elements found in bacteria, but not all genetic elements in bacteria are considered genes. For example, some DNA sequences may not encode functional products and are therefore not considered genes. Additionally, some bacterial genes may be plasmid-borne or phage-borne, rather than being located on the bacterial chromosome.

An open reading frame (ORF) is a continuous stretch of DNA or RNA sequence that has the potential to be translated into a protein. It begins with a start codon (usually "ATG" in DNA, which corresponds to "AUG" in RNA) and ends with a stop codon ("TAA", "TAG", or "TGA" in DNA; "UAA", "UAG", or "UGA" in RNA). The sequence between these two points is called a coding sequence (CDS), which, when transcribed into mRNA and translated into amino acids, forms a polypeptide chain.

In eukaryotic cells, ORFs can be located in either protein-coding genes or non-coding regions of the genome. In prokaryotic cells, multiple ORFs may be present on a single strand of DNA, often organized into operons that are transcribed together as a single mRNA molecule.

It's important to note that not all ORFs necessarily represent functional proteins; some may be pseudogenes or result from errors in genome annotation. Therefore, additional experimental evidence is typically required to confirm the expression and functionality of a given ORF.

A large archaeal ribosomal subunit refers to the larger of the two components that make up the archaeal ribosome, which is the complex molecular machine responsible for protein synthesis in archaea. The large ribosomal subunit plays a crucial role in the elongation phase of translation, where it helps catalyze the formation of peptide bonds between amino acids during protein synthesis.

The large ribosomal subunit of archaea is composed of ribosomal RNA (rRNA) and proteins. Specifically, the archaeal large ribosomal subunit contains a 23S rRNA molecule, a 5S rRNA molecule, and around 30-40 different proteins. These components are organized into several distinct structural domains, including the central protuberance, the L1 stalk, and the peptidyl transferase center (PTC), which is where peptide bond formation occurs.

It's worth noting that while archaeal ribosomes share some similarities with eukaryotic ribosomes, they are more closely related to bacterial ribosomes in terms of their structure and composition. However, the large ribosomal subunit of archaea is still distinct from both bacterial and eukaryotic subunits in its specific rRNA sequences and protein composition.

DNA-directed DNA polymerase is a type of enzyme that synthesizes new strands of DNA by adding nucleotides to an existing DNA template in a 5' to 3' direction. These enzymes are essential for DNA replication, repair, and recombination. They require a single-stranded DNA template, a primer with a free 3' hydroxyl group, and the four deoxyribonucleoside triphosphates (dNTPs) as substrates to carry out the polymerization reaction.

DNA polymerases also have proofreading activity, which allows them to correct errors that occur during DNA replication by removing mismatched nucleotides and replacing them with the correct ones. This helps ensure the fidelity of the genetic information passed from one generation to the next.

There are several different types of DNA polymerases, each with specific functions and characteristics. For example, DNA polymerase I is involved in both DNA replication and repair, while DNA polymerase III is the primary enzyme responsible for DNA replication in bacteria. In eukaryotic cells, DNA polymerase alpha, beta, gamma, delta, and epsilon have distinct roles in DNA replication, repair, and maintenance.

Aldehyde-lyases are a class of enzymes that catalyze the breakdown or synthesis of molecules involving an aldehyde group through a reaction known as lyase cleavage. This type of reaction results in the removal of a molecule, typically water or carbon dioxide, from the substrate.

In the case of aldehyde-lyases, these enzymes specifically catalyze reactions that involve the conversion of an aldehyde into a carboxylic acid or vice versa. These enzymes are important in various metabolic pathways and play a crucial role in the biosynthesis and degradation of several biomolecules, including carbohydrates, amino acids, and lipids.

The systematic name for this class of enzymes is "ald(e)hyde-lyases." They are classified under EC number 4.3.1 in the Enzyme Commission (EC) system.

Quaternary protein structure refers to the arrangement and interaction of multiple folded protein molecules in a multi-subunit complex. These subunits can be identical or different forms of the same protein or distinctly different proteins that associate to form a functional complex. The quaternary structure is held together by non-covalent interactions, such as hydrogen bonds, ionic bonds, and van der Waals forces. Understanding quaternary structure is crucial for comprehending the function, regulation, and assembly of many protein complexes involved in various cellular processes.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

Sulfur is not typically referred to in the context of a medical definition, as it is an element found in nature and not a specific medical condition or concept. However, sulfur does have some relevance to certain medical topics:

* Sulfur is an essential element that is a component of several amino acids (the building blocks of proteins) and is necessary for the proper functioning of enzymes and other biological processes in the body.
* Sulfur-containing compounds, such as glutathione, play important roles in antioxidant defense and detoxification in the body.
* Some medications and supplements contain sulfur or sulfur-containing compounds, such as dimethyl sulfoxide (DMSO), which is used topically for pain relief and inflammation.
* Sulfur baths and other forms of sulfur-based therapies have been used historically in alternative medicine to treat various conditions, although their effectiveness is not well-established by scientific research.

It's important to note that while sulfur itself is not a medical term, it can be relevant to certain medical topics and should be discussed with a healthcare professional if you have any questions or concerns about its use in medications, supplements, or therapies.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Neoprene is not a medical term, but it is a material that is used in some medical applications. Neoprene is a type of synthetic rubber that is known for its flexibility, durability, and resistance to heat, water, and chemicals. It is often used in the manufacture of medical devices such as braces, supports, and protective gear.

In medical terms, neoprene may be referred to as a component of a device or material used in medical applications. For example, a neoprene sleeve may be used as a compression garment for venous insufficiency or lymphedema management. Neoprene is also sometimes used in the manufacture of medical gloves and other protective equipment due to its resistance to chemicals and other substances.

However, it's important to note that some people may have allergic reactions to neoprene, causing skin irritation or other symptoms. Therefore, healthcare providers should consider patients' individual needs and potential allergies when selecting medical devices made of neoprene or other materials.

A ribosome is a complex molecular machine found in all living cells that translates messenger RNA (mRNA) into proteins. Ribosomes are composed of two subunits: a small subunit and a large subunit. The small subunit is responsible for recognizing and binding to the mRNA, as well as decoding the genetic information it contains.

Archaeal ribosomes are similar in structure and function to eukaryotic ribosomes, but they have some distinct differences in their composition and sequence. Archaeal small ribosomal subunits, like those of bacteria, are composed of a 16S rRNA molecule and approximately 20 proteins. However, the archaeal small ribosomal subunit has a unique structure and composition that is distinct from both bacterial and eukaryotic small ribosomal subunits.

The small ribosomal subunit of Archaea is referred to as the "small, archaeal" subunit. It plays a crucial role in the initiation of protein synthesis by recognizing and binding to the Shine-Dalgarno sequence in the mRNA, which helps position the start codon for translation. The small, archaeal ribosomal subunit also contains the decoding center, where the genetic information in the mRNA is translated into a corresponding amino acid sequence during protein synthesis.

Overall, the small, archaeal ribosomal subunit is an essential component of the archaeal translational machinery, responsible for accurately and efficiently decoding genetic information and initiating the synthesis of new proteins.

I'm sorry for any confusion, but Tetrathionic Acid is not a medical term. It is a chemical compound with the formula S4O62-. It's an acidic oxyanion of sulfur with the sulfur in the +5 oxidation state. It is not related to human health or medicine directly. If you have any questions about a medical topic, I'd be happy to help with that instead!

CRISPR-Cas systems are adaptive immune systems found in bacteria and archaea. CRISPR stands for "Clustered Regularly Interspaced Short Palindromic Repeats," which are repeating sequences of DNA found in the genomes of these microorganisms. Cas stands for "CRISPR-associated proteins," which work together with the CRISPR sequences to provide immunity against foreign genetic elements, such as viruses and plasmids.

The CRISPR-Cas system functions by incorporating short segments of DNA from invading genetic elements into the CRISPR array within the microorganism's genome. These incorporated sequences are then transcribed and processed into small RNA molecules called guide RNAs. The Cas proteins, in complex with the guide RNA, recognize and bind to complementary sequences in the invading genetic element, leading to its cleavage and degradation.

The CRISPR-Cas system has been harnessed for use as a powerful tool in genome editing, allowing researchers to precisely modify DNA sequences in various organisms, including humans. This technology holds great promise for treating genetic diseases, improving crops, and developing new therapies for infectious diseases.

Phylogeny is the evolutionary history and relationship among biological entities, such as species or genes, based on their shared characteristics. In other words, it refers to the branching pattern of evolution that shows how various organisms have descended from a common ancestor over time. Phylogenetic analysis involves constructing a tree-like diagram called a phylogenetic tree, which depicts the inferred evolutionary relationships among organisms or genes based on molecular sequence data or other types of characters. This information is crucial for understanding the diversity and distribution of life on Earth, as well as for studying the emergence and spread of diseases.

Electron Spin Resonance (ESR) Spectroscopy, also known as Electron Paramagnetic Resonance (EPR) Spectroscopy, is a technique used to investigate materials with unpaired electrons. It is based on the principle of absorption of energy by the unpaired electrons when they are exposed to an external magnetic field and microwave radiation.

In this technique, a sample is placed in a magnetic field and microwave radiation is applied. The unpaired electrons in the sample absorb energy and change their spin state when the energy of the microwaves matches the energy difference between the spin states. This absorption of energy is recorded as a function of the magnetic field strength, producing an ESR spectrum.

ESR spectroscopy can provide information about the number, type, and behavior of unpaired electrons in a sample, as well as the local environment around the electron. It is widely used in physics, chemistry, and biology to study materials such as free radicals, transition metal ions, and defects in solids.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Leucine-Responsive Regulatory Protein (LRP) is not a well-established medical term, but it is a term used in biochemistry and molecular biology. It generally refers to a protein that is involved in the regulation of gene expression in response to leucine, an essential amino acid.

Leucine is known to stimulate protein synthesis and inhibit protein degradation in cells. LRP plays a crucial role in this process by acting as a sensor for leucine levels in the cell. When leucine levels are high, LRP becomes activated and binds to specific DNA sequences called response elements, which are located in the promoter regions of genes that are involved in protein synthesis and degradation. This binding leads to the activation or repression of these genes, thereby regulating protein metabolism in the cell.

In summary, Leucine-Responsive Regulatory Protein is a protein that regulates gene expression in response to leucine levels, playing a critical role in the regulation of protein synthesis and degradation in cells.

Alpha-glucosidases are a group of enzymes that break down complex carbohydrates into simpler sugars, such as glucose, by hydrolyzing the alpha-1,4 and alpha-1,6 glycosidic bonds in oligosaccharides, disaccharides, and polysaccharides. These enzymes are located on the brush border of the small intestine and play a crucial role in carbohydrate digestion and absorption.

Inhibitors of alpha-glucosidases, such as acarbose and miglitol, are used in the treatment of type 2 diabetes to slow down the digestion and absorption of carbohydrates, which helps to reduce postprandial glucose levels and improve glycemic control.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

DNA replication is the biological process by which DNA makes an identical copy of itself during cell division. It is a fundamental mechanism that allows genetic information to be passed down from one generation of cells to the next. During DNA replication, each strand of the double helix serves as a template for the synthesis of a new complementary strand. This results in the creation of two identical DNA molecules. The enzymes responsible for DNA replication include helicase, which unwinds the double helix, and polymerase, which adds nucleotides to the growing strands.

Nucleic acid conformation refers to the three-dimensional structure that nucleic acids (DNA and RNA) adopt as a result of the bonding patterns between the atoms within the molecule. The primary structure of nucleic acids is determined by the sequence of nucleotides, while the conformation is influenced by factors such as the sugar-phosphate backbone, base stacking, and hydrogen bonding.

Two common conformations of DNA are the B-form and the A-form. The B-form is a right-handed helix with a diameter of about 20 Å and a pitch of 34 Å, while the A-form has a smaller diameter (about 18 Å) and a shorter pitch (about 25 Å). RNA typically adopts an A-form conformation.

The conformation of nucleic acids can have significant implications for their function, as it can affect their ability to interact with other molecules such as proteins or drugs. Understanding the conformational properties of nucleic acids is therefore an important area of research in molecular biology and medicine.

Prokaryotic initiation factors are a group of proteins that play an essential role in the initiation phase of protein synthesis in prokaryotes, such as bacteria. These factors help to assemble the ribosome complex and facilitate the binding of messenger RNA (mRNA) and transfer RNA (tRNA) during the start of translation, the process by which genetic information encoded in mRNA is converted into a protein sequence.

There are three main prokaryotic initiation factors:

1. IF1 (InfA): This factor binds to the 30S ribosomal subunit and prevents it from prematurely binding to the 50S ribosomal subunit before the mRNA is properly positioned. It also helps in the correct positioning of the initiator tRNA (tRNAi) during initiation.

2. IF2 (InfB): This factor plays a crucial role in recognizing and binding the initiator tRNA to the 30S ribosomal subunit, forming the 70S initiation complex. It also hydrolyzes GTP during this process, which provides energy for the reaction.

3. IF3 (InfC): This factor helps in the dissociation of the 70S ribosome into its individual 30S and 50S subunits after translation is complete. During initiation, it binds to the 30S subunit and prevents incorrect mRNA binding while promoting the correct positioning of the initiator tRNA.

These prokaryotic initiation factors work together to ensure accurate and efficient protein synthesis in bacteria and other prokaryotes.

Holliday junction resolvases are a type of enzyme that are involved in the process of genetic recombination. They are named after Robin Holliday, who first proposed the existence of a structure called a Holliday junction during genetic recombination.

A Holliday junction is a four-way DNA structure that forms when two DNA molecules exchange genetic material during recombination. The junction is held together by hydrogen bonds between complementary base pairs, and it can move along the DNA molecules through a process called branch migration.

Holliday junction resolvases are responsible for cleaving the DNA strands at the Holliday junction, resolving the structure into two separate DNA molecules. They do this by introducing nicks in the phosphodiester backbone of the DNA strands on either side of the junction and then joining the broken ends together. This results in the exchange of genetic material between the two original DNA molecules.

There are several different types of Holliday junction resolvases, including the bacterial RuvC and RecU enzymes, as well as the eukaryotic Flap endonuclease 1 (FEN1) and XPF/ERCC1 complexes. These enzymes have different specificities for cleaving the DNA strands at the Holliday junction, but they all play important roles in ensuring that genetic recombination occurs accurately and efficiently.

Selenomethionine is an organic form of selenium, which is an essential trace element in human nutrition. It is incorporated into proteins in place of methionine, one of the 20 standard amino acids, and functions as an antioxidant by helping to prevent cellular damage from free radicals. Selenomethionine can be found in a variety of foods, including brazil nuts, fish, meat, and whole grains, and is also available as a dietary supplement.

Spermidine synthase is an enzyme (EC 2.5.1.16) that catalyzes the synthesis of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM). This reaction is a part of the polyamine biosynthetic pathway, which plays a crucial role in cell growth and differentiation.

The reaction catalyzed by spermidine synthase can be represented as follows:
putrescine + dcSAM → spermidine + S-adenosylhomocysteine

In humans, there are two isoforms of spermidine synthase, namely, SRM and SMS. These isoforms share a common catalytic mechanism but differ in their subcellular localization and regulation. Mutations in the genes encoding spermidine synthase have been associated with certain diseases, such as cancer and neurological disorders.

Orotic acid, also known as pyrmidine carboxylic acid, is a organic compound that plays a role in the metabolic pathway for the biosynthesis of pyrimidines, which are nitrogenous bases found in nucleotides and nucleic acids such as DNA and RNA. Orotic acid is not considered to be a vitamin, but it is sometimes referred to as vitamin B13 or B15, although these designations are not widely recognized by the scientific community.

In the body, orotic acid is converted into orotidine monophosphate (OMP) by the enzyme orotate phosphoribosyltransferase. OMP is then further metabolized to form uridine monophosphate (UMP), a pyrimidine nucleotide that is an important precursor for the synthesis of RNA and other molecules.

Elevated levels of orotic acid in the urine, known as orotic aciduria, can be a sign of certain genetic disorders that affect the metabolism of pyrimidines. These conditions can lead to an accumulation of orotic acid and other pyrimidine precursors in the body, which can cause a range of symptoms including developmental delays, neurological problems, and kidney stones. Treatment for these disorders typically involves dietary restrictions and supplementation with nucleotides or nucleosides to help support normal pyrimidine metabolism.

Dextrins are a group of carbohydrates that are produced by the hydrolysis of starches. They are made up of shorter chains of glucose molecules than the original starch, and their molecular weight and physical properties can vary depending on the degree of hydrolysis. Dextrins are often used in food products as thickeners, stabilizers, and texturizers, and they also have applications in industry as adhesives and binders. In a medical context, dextrins may be used as a source of calories for patients who have difficulty digesting other types of carbohydrates.

Helix-Turn-Helix (HTH) motif is a common structural feature found in DNA-binding proteins, where a pair of alpha-helices are connected by a short loop or "turn." The second helix, often referred to as the recognition helix, fits into the major groove of the DNA double helix and makes specific contacts with the bases, thereby determining the binding specificity of the protein to its target DNA sequence. This motif is widely found in transcription factors and other regulatory proteins that control gene expression in all living organisms.

Dimerization is a process in which two molecules, usually proteins or similar structures, bind together to form a larger complex. This can occur through various mechanisms, such as the formation of disulfide bonds, hydrogen bonding, or other non-covalent interactions. Dimerization can play important roles in cell signaling, enzyme function, and the regulation of gene expression.

In the context of medical research and therapy, dimerization is often studied in relation to specific proteins that are involved in diseases such as cancer. For example, some drugs have been developed to target and inhibit the dimerization of certain proteins, with the goal of disrupting their function and slowing or stopping the progression of the disease.

23S Ribosomal RNA (rRNA) is a type of rRNA that is a component of the large ribosomal subunit in both prokaryotic and eukaryotic cells. In prokaryotes, the large ribosomal subunit contains 50S, which consists of 23S rRNA, 5S rRNA, and around 33 proteins. The 23S rRNA plays a crucial role in the decoding of mRNA during protein synthesis and also participates in the formation of the peptidyl transferase center, where peptide bonds are formed between amino acids.

The 23S rRNA is a long RNA molecule that contains both coding and non-coding regions. It has a complex secondary structure, which includes several domains and subdomains, as well as numerous stem-loop structures. These structures are important for the proper functioning of the ribosome during protein synthesis.

In addition to its role in protein synthesis, 23S rRNA has been used as a target for antibiotics that inhibit bacterial growth. For example, certain antibiotics bind to specific regions of the 23S rRNA and interfere with the function of the ribosome, thereby preventing bacterial protein synthesis and growth. However, because eukaryotic cells do not have a 23S rRNA equivalent, these antibiotics are generally not toxic to human cells.

Methanococcales is an order of methanogenic archaea within the kingdom Euryarchaeota. These are microorganisms that produce methane as a metabolic byproduct in anaerobic environments. Members of this order are distinguished by their ability to generate energy through the reduction of carbon dioxide with hydrogen gas, a process known as CO2 reduction. They are typically found in marine sediments, deep-sea vents, and other extreme habitats. The most well-known genus within Methanococcales is Methanococcus, which includes several species that are capable of living at relatively high temperatures and pressures.

Tetramethylphenylenediamine (TMPD) is not typically considered a medical term, but it is a chemical compound that is used in some scientific and research contexts. It's a type of aromatic amine, which is a class of organic compounds characterized by the presence of one or more amino groups (-NH2) attached to an aromatic hydrocarbon ring.

In biochemistry and molecular biology, TMPD is sometimes used as an electron carrier in experiments that involve redox reactions, such as those that occur during cellular respiration. It can also be used as a catalyst or reagent in various chemical reactions. However, it's important to note that TMPD is not a substance that is typically encountered in medical practice or patient care.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

DNA Sequence Analysis is the systematic determination of the order of nucleotides in a DNA molecule. It is a critical component of modern molecular biology, genetics, and genetic engineering. The process involves determining the exact order of the four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - in a DNA molecule or fragment. This information is used in various applications such as identifying gene mutations, studying evolutionary relationships, developing molecular markers for breeding, and diagnosing genetic diseases.

The process of DNA Sequence Analysis typically involves several steps, including DNA extraction, PCR amplification (if necessary), purification, sequencing reaction, and electrophoresis. The resulting data is then analyzed using specialized software to determine the exact sequence of nucleotides.

In recent years, high-throughput DNA sequencing technologies have revolutionized the field of genomics, enabling the rapid and cost-effective sequencing of entire genomes. This has led to an explosion of genomic data and new insights into the genetic basis of many diseases and traits.

DNA-binding proteins are a type of protein that have the ability to bind to DNA (deoxyribonucleic acid), the genetic material of organisms. These proteins play crucial roles in various biological processes, such as regulation of gene expression, DNA replication, repair and recombination.

The binding of DNA-binding proteins to specific DNA sequences is mediated by non-covalent interactions, including electrostatic, hydrogen bonding, and van der Waals forces. The specificity of binding is determined by the recognition of particular nucleotide sequences or structural features of the DNA molecule.

DNA-binding proteins can be classified into several categories based on their structure and function, such as transcription factors, histones, and restriction enzymes. Transcription factors are a major class of DNA-binding proteins that regulate gene expression by binding to specific DNA sequences in the promoter region of genes and recruiting other proteins to modulate transcription. Histones are DNA-binding proteins that package DNA into nucleosomes, the basic unit of chromatin structure. Restriction enzymes are DNA-binding proteins that recognize and cleave specific DNA sequences, and are widely used in molecular biology research and biotechnology applications.

A plasmid is a small, circular, double-stranded DNA molecule that is separate from the chromosomal DNA of a bacterium or other organism. Plasmids are typically not essential for the survival of the organism, but they can confer beneficial traits such as antibiotic resistance or the ability to degrade certain types of pollutants.

Plasmids are capable of replicating independently of the chromosomal DNA and can be transferred between bacteria through a process called conjugation. They often contain genes that provide resistance to antibiotics, heavy metals, and other environmental stressors. Plasmids have also been engineered for use in molecular biology as cloning vectors, allowing scientists to replicate and manipulate specific DNA sequences.

Plasmids are important tools in genetic engineering and biotechnology because they can be easily manipulated and transferred between organisms. They have been used to produce vaccines, diagnostic tests, and genetically modified organisms (GMOs) for various applications, including agriculture, medicine, and industry.

Malate Synthase is a key enzyme in the gluconeogenesis pathway and the glyoxylate cycle, which are present in many organisms including plants, bacteria, and parasites. The glyoxylate cycle is a variation of the citric acid cycle (Krebs cycle) that allows these organisms to convert two-carbon molecules into four-carbon molecules, bypassing steps that require oxygen.

Malate Synthase catalyzes the reaction between glyoxylate and acetyl-CoA to produce malate, a four-carbon compound. This enzyme plays a crucial role in enabling these organisms to utilize fatty acids as a carbon source for growth and energy production, particularly under conditions where oxygen is limited or absent. In humans, Malate Synthase is not typically found, but its presence can indicate certain parasitic infections or metabolic disorders.

Hydrolysis is a chemical process, not a medical one. However, it is relevant to medicine and biology.

Hydrolysis is the breakdown of a chemical compound due to its reaction with water, often resulting in the formation of two or more simpler compounds. In the context of physiology and medicine, hydrolysis is a crucial process in various biological reactions, such as the digestion of food molecules like proteins, carbohydrates, and fats. Enzymes called hydrolases catalyze these hydrolysis reactions to speed up the breakdown process in the body.

X-ray diffraction (XRD) is not strictly a medical definition, but it is a technique commonly used in the field of medical research and diagnostics. XRD is a form of analytical spectroscopy that uses the phenomenon of X-ray diffraction to investigate the crystallographic structure of materials. When a beam of X-rays strikes a crystal, it is scattered in specific directions and with specific intensities that are determined by the arrangement of atoms within the crystal. By measuring these diffraction patterns, researchers can determine the crystal structures of various materials, including biological macromolecules such as proteins and viruses.

In the medical field, XRD is often used to study the structure of drugs and drug candidates, as well as to analyze the composition and structure of tissues and other biological samples. For example, XRD can be used to investigate the crystal structures of calcium phosphate minerals in bone tissue, which can provide insights into the mechanisms of bone formation and disease. Additionally, XRD is sometimes used in the development of new medical imaging techniques, such as phase-contrast X-ray imaging, which has the potential to improve the resolution and contrast of traditional X-ray images.

Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.

Bacterial proteins can be classified into different categories based on their function, such as:

1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.

Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.

Acid anhydride hydrolases are a class of enzymes that catalyze the hydrolysis (breakdown) of acid anhydrides, which are chemical compounds formed by the reaction between two carboxylic acids. This reaction results in the formation of a molecule of water and the release of a new carboxylic acid.

Acid anhydride hydrolases play important roles in various biological processes, including the metabolism of lipids, carbohydrates, and amino acids. They are also involved in the regulation of intracellular pH and the detoxification of xenobiotics (foreign substances).

Examples of acid anhydride hydrolases include esterases, lipases, and phosphatases. These enzymes have different substrate specificities and catalytic mechanisms, but they all share the ability to hydrolyze acid anhydrides.

The term "acid anhydride hydrolase" is often used interchangeably with "esterase," although not all esterases are capable of hydrolyzing acid anhydrides.

Glucose dehydrogenases (GDHs) are a group of enzymes that catalyze the oxidation of glucose to generate gluconic acid or glucuronic acid. This reaction involves the transfer of electrons from glucose to an electron acceptor, most commonly nicotinamide adenine dinucleotide (NAD+) or phenazine methosulfate (PMS).

GDHs are widely distributed in nature and can be found in various organisms, including bacteria, fungi, plants, and animals. They play important roles in different biological processes, such as glucose metabolism, energy production, and detoxification of harmful substances. Based on their cofactor specificity, GDHs can be classified into two main types: NAD(P)-dependent GDHs and PQQ-dependent GDHs.

NAD(P)-dependent GDHs use NAD+ or NADP+ as a cofactor to oxidize glucose to glucono-1,5-lactone, which is then hydrolyzed to gluconic acid by an accompanying enzyme. These GDHs are involved in various metabolic pathways, such as the Entner-Doudoroff pathway and the oxidative pentose phosphate pathway.

PQQ-dependent GDHs, on the other hand, use pyrroloquinoline quinone (PQQ) as a cofactor to catalyze the oxidation of glucose to gluconic acid directly. These GDHs are typically found in bacteria and play a role in energy production and detoxification.

Overall, glucose dehydrogenases are essential enzymes that contribute to the maintenance of glucose homeostasis and energy balance in living organisms.

Winged-helix transcription factors are a family of proteins involved in the regulation of gene expression. They are called winged-helix because of their unique structure, which includes a helix-turn-helix motif and two "wing" regions that are involved in DNA binding. These transcription factors play crucial roles in various biological processes such as development, differentiation, and metabolism by regulating the expression of specific genes. Some examples of winged-helix transcription factors include HNF-3 (hepatocyte nuclear factor 3), FOXP3 (forkhead box P3), and NFAT (nuclear factor of activated T-cells). Mutations in these proteins have been associated with various human diseases, including diabetes, cancer, and immunodeficiency.

Adenosine triphosphatases (ATPases) are a group of enzymes that catalyze the conversion of adenosine triphosphate (ATP) into adenosine diphosphate (ADP) and inorganic phosphate. This reaction releases energy, which is used to drive various cellular processes such as muscle contraction, transport of ions across membranes, and synthesis of proteins and nucleic acids.

ATPases are classified into several types based on their structure, function, and mechanism of action. Some examples include:

1. P-type ATPases: These ATPases form a phosphorylated intermediate during the reaction cycle and are involved in the transport of ions across membranes, such as the sodium-potassium pump and calcium pumps.
2. F-type ATPases: These ATPases are found in mitochondria, chloroplasts, and bacteria, and are responsible for generating a proton gradient across the membrane, which is used to synthesize ATP.
3. V-type ATPases: These ATPases are found in vacuolar membranes and endomembranes, and are involved in acidification of intracellular compartments.
4. A-type ATPases: These ATPases are found in the plasma membrane and are involved in various functions such as cell signaling and ion transport.

Overall, ATPases play a crucial role in maintaining the energy balance of cells and regulating various physiological processes.

A multigene family is a group of genetically related genes that share a common ancestry and have similar sequences or structures. These genes are arranged in clusters on a chromosome and often encode proteins with similar functions. They can arise through various mechanisms, including gene duplication, recombination, and transposition. Multigene families play crucial roles in many biological processes, such as development, immunity, and metabolism. Examples of multigene families include the globin genes involved in oxygen transport, the immune system's major histocompatibility complex (MHC) genes, and the cytochrome P450 genes associated with drug metabolism.

Sequence homology in nucleic acids refers to the similarity or identity between the nucleotide sequences of two or more DNA or RNA molecules. It is often used as a measure of biological relationship between genes, organisms, or populations. High sequence homology suggests a recent common ancestry or functional constraint, while low sequence homology may indicate a more distant relationship or different functions.

Nucleic acid sequence homology can be determined by various methods such as pairwise alignment, multiple sequence alignment, and statistical analysis. The degree of homology is typically expressed as a percentage of identical or similar nucleotides in a given window of comparison.

It's important to note that the interpretation of sequence homology depends on the biological context and the evolutionary distance between the sequences compared. Therefore, functional and experimental validation is often necessary to confirm the significance of sequence homology.

Coenzymes are small organic molecules that assist enzymes in catalyzing chemical reactions within cells. They typically act as carriers of specific atoms or groups of atoms during enzymatic reactions, facilitating the conversion of substrates into products. Coenzymes often bind temporarily to enzymes at the active site, forming an enzyme-coenzyme complex.

Coenzymes are usually derived from vitamins or minerals and are essential for maintaining proper metabolic functions in the body. Examples of coenzymes include nicotinamide adenine dinucleotide (NAD+), flavin adenine dinucleotide (FAD), and coenzyme A (CoA). When a coenzyme is used up in a reaction, it must be regenerated or replaced for the enzyme to continue functioning.

In summary, coenzymes are vital organic compounds that work closely with enzymes to facilitate biochemical reactions, ensuring the smooth operation of various metabolic processes within living organisms.

In medical terms, acids refer to a class of chemicals that have a pH less than 7 and can donate protons (hydrogen ions) in chemical reactions. In the context of human health, acids are an important part of various bodily functions, such as digestion. However, an imbalance in acid levels can lead to medical conditions. For example, an excess of hydrochloric acid in the stomach can cause gastritis or peptic ulcers, while an accumulation of lactic acid due to strenuous exercise or decreased blood flow can lead to muscle fatigue and pain.

Additionally, in clinical laboratory tests, certain substances may be tested for their "acidity" or "alkalinity," which is measured using a pH scale. This information can help diagnose various medical conditions, such as kidney disease or diabetes.

Biological toxins are poisonous substances that are produced by living organisms such as bacteria, plants, and animals. They can cause harm to humans, animals, or the environment. Biological toxins can be classified into different categories based on their mode of action, such as neurotoxins (affecting the nervous system), cytotoxins (damaging cells), and enterotoxins (causing intestinal damage).

Examples of biological toxins include botulinum toxin produced by Clostridium botulinum bacteria, tetanus toxin produced by Clostridium tetani bacteria, ricin toxin from the castor bean plant, and saxitoxin produced by certain types of marine algae.

Biological toxins can cause a range of symptoms depending on the type and amount of toxin ingested or exposed to, as well as the route of exposure (e.g., inhalation, ingestion, skin contact). They can cause illnesses ranging from mild to severe, and some can be fatal if not treated promptly and effectively.

Prevention and control measures for biological toxins include good hygiene practices, vaccination against certain toxin-producing bacteria, avoidance of contaminated food or water sources, and personal protective equipment (PPE) when handling or working with potential sources of toxins.

Circular dichroism (CD) is a technique used in physics and chemistry to study the structure of molecules, particularly large biological molecules such as proteins and nucleic acids. It measures the difference in absorption of left-handed and right-handed circularly polarized light by a sample. This difference in absorption can provide information about the three-dimensional structure of the molecule, including its chirality or "handedness."

In more technical terms, CD is a form of spectroscopy that measures the differential absorption of left and right circularly polarized light as a function of wavelength. The CD signal is measured in units of millidegrees (mdeg) and can be positive or negative, depending on the type of chromophore and its orientation within the molecule.

CD spectra can provide valuable information about the secondary and tertiary structure of proteins, as well as the conformation of nucleic acids. For example, alpha-helical proteins typically exhibit a strong positive band near 190 nm and two negative bands at around 208 nm and 222 nm, while beta-sheet proteins show a strong positive band near 195 nm and two negative bands at around 217 nm and 175 nm.

CD spectroscopy is a powerful tool for studying the structural changes that occur in biological molecules under different conditions, such as temperature, pH, or the presence of ligands or other molecules. It can also be used to monitor the folding and unfolding of proteins, as well as the binding of drugs or other small molecules to their targets.

Protein folding is the process by which a protein molecule naturally folds into its three-dimensional structure, following the synthesis of its amino acid chain. This complex process is determined by the sequence and properties of the amino acids, as well as various environmental factors such as temperature, pH, and the presence of molecular chaperones. The final folded conformation of a protein is crucial for its proper function, as it enables the formation of specific interactions between different parts of the molecule, which in turn define its biological activity. Protein misfolding can lead to various diseases, including neurodegenerative disorders such as Alzheimer's and Parkinson's disease.

I'm sorry for any confusion, but "thermodynamics" is not a term that has a specific medical definition. It is a branch of physics that deals with the relationships between heat and other forms of energy. However, the principles of thermodynamics can be applied to biological systems, including those in the human body, such as in the study of metabolism or muscle function. But in a medical context, "thermodynamics" would not be a term used independently as a diagnosis, treatment, or any medical condition.

Bacterial DNA refers to the genetic material found in bacteria. It is composed of a double-stranded helix containing four nucleotide bases - adenine (A), thymine (T), guanine (G), and cytosine (C) - that are linked together by phosphodiester bonds. The sequence of these bases in the DNA molecule carries the genetic information necessary for the growth, development, and reproduction of bacteria.

Bacterial DNA is circular in most bacterial species, although some have linear chromosomes. In addition to the main chromosome, many bacteria also contain small circular pieces of DNA called plasmids that can carry additional genes and provide resistance to antibiotics or other environmental stressors.

Unlike eukaryotic cells, which have their DNA enclosed within a nucleus, bacterial DNA is present in the cytoplasm of the cell, where it is in direct contact with the cell's metabolic machinery. This allows for rapid gene expression and regulation in response to changing environmental conditions.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

Secondary protein structure refers to the local spatial arrangement of amino acid chains in a protein, typically described as regular repeating patterns held together by hydrogen bonds. The two most common types of secondary structures are the alpha-helix (α-helix) and the beta-pleated sheet (β-sheet). In an α-helix, the polypeptide chain twists around itself in a helical shape, with each backbone atom forming a hydrogen bond with the fourth amino acid residue along the chain. This forms a rigid rod-like structure that is resistant to bending or twisting forces. In β-sheets, adjacent segments of the polypeptide chain run parallel or antiparallel to each other and are connected by hydrogen bonds, forming a pleated sheet-like arrangement. These secondary structures provide the foundation for the formation of tertiary and quaternary protein structures, which determine the overall three-dimensional shape and function of the protein.

Beta-glucosidase is an enzyme that breaks down certain types of complex sugars, specifically those that contain a beta-glycosidic bond. This enzyme is found in various organisms, including humans, and plays a role in the digestion of some carbohydrates, such as cellulose and other plant-based materials.

In the human body, beta-glucosidase is produced by the lysosomes, which are membrane-bound organelles found within cells that help break down and recycle various biological molecules. Beta-glucosidase is involved in the breakdown of glycolipids and gangliosides, which are complex lipids that contain sugar molecules.

Deficiencies in beta-glucosidase activity can lead to certain genetic disorders, such as Gaucher disease, in which there is an accumulation of glucocerebrosidase, a type of glycolipid, within the lysosomes. This can result in various symptoms, including enlargement of the liver and spleen, anemia, and bone pain.

Deoxyribonucleic acid (DNA) is the genetic material present in the cells of organisms where it is responsible for the storage and transmission of hereditary information. DNA is a long molecule that consists of two strands coiled together to form a double helix. Each strand is made up of a series of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - that are linked together by phosphate and sugar groups. The sequence of these bases along the length of the molecule encodes genetic information, with A always pairing with T and C always pairing with G. This base-pairing allows for the replication and transcription of DNA, which are essential processes in the functioning and reproduction of all living organisms.

DNA footprinting is a laboratory technique used to identify specific DNA-protein interactions and map the binding sites of proteins on a DNA molecule. This technique involves the use of enzymes or chemicals that can cleave the DNA strand, but are prevented from doing so when a protein is bound to the DNA. By comparing the pattern of cuts in the presence and absence of the protein, researchers can identify the regions of the DNA where the protein binds.

The process typically involves treating the DNA-protein complex with a chemical or enzymatic agent that cleaves the DNA at specific sequences or sites. After the reaction is stopped, the DNA is separated into single strands and analyzed using techniques such as gel electrophoresis to visualize the pattern of cuts. The regions of the DNA where protein binding has occurred are protected from cleavage and appear as gaps or "footprints" in the pattern of cuts.

DNA footprinting is a valuable tool for studying gene regulation, as it can provide insights into how proteins interact with specific DNA sequences to control gene expression. It can also be used to study protein-DNA interactions involved in processes such as DNA replication, repair, and recombination.

Genetic transcription is the process by which the information in a strand of DNA is used to create a complementary RNA molecule. This process is the first step in gene expression, where the genetic code in DNA is converted into a form that can be used to produce proteins or functional RNAs.

During transcription, an enzyme called RNA polymerase binds to the DNA template strand and reads the sequence of nucleotide bases. As it moves along the template, it adds complementary RNA nucleotides to the growing RNA chain, creating a single-stranded RNA molecule that is complementary to the DNA template strand. Once transcription is complete, the RNA molecule may undergo further processing before it can be translated into protein or perform its functional role in the cell.

Transcription can be either "constitutive" or "regulated." Constitutive transcription occurs at a relatively constant rate and produces essential proteins that are required for basic cellular functions. Regulated transcription, on the other hand, is subject to control by various intracellular and extracellular signals, allowing cells to respond to changing environmental conditions or developmental cues.

Protein denaturation is a process in which the native structure of a protein is altered, leading to loss of its biological activity. This can be caused by various factors such as changes in temperature, pH, or exposure to chemicals or radiation. The three-dimensional shape of a protein is crucial for its function, and denaturation causes the protein to lose this shape, resulting in impaired or complete loss of function. Denaturation is often irreversible and can lead to the aggregation of proteins, which can have negative effects on cellular function and can contribute to diseases such as Alzheimer's and Parkinson's.

Purine-nucleoside phosphorylase (PNP) is an enzyme that plays a crucial role in the metabolism of purines, which are essential components of nucleic acids (DNA and RNA). The medical definition of 'Purine-Nucleoside Phosphorylase' refers to the physiological function of this enzyme in the human body.

PNP is responsible for catalyzing the phosphorolytic cleavage of purine nucleosides, such as inosine and guanosine, into their respective purine bases (hypoxanthine and guanine) and ribose-1-phosphate. This reaction is essential for the recycling and salvage of purine bases, allowing the body to conserve energy and resources needed for de novo purine biosynthesis.

In a clinical or medical context, deficiencies in PNP activity can lead to serious consequences, particularly affecting the immune system and the nervous system. A genetic disorder called Purine-Nucleoside Phosphorylase Deficiency (PNP Deficiency) is characterized by significantly reduced or absent PNP enzyme activity, leading to an accumulation of toxic purine nucleosides and deoxypurine nucleosides. This accumulation can cause severe combined immunodeficiency (SCID), neurological impairments, and other complications, making it a critical area of study in medical research.

Sequence homology is a term used in molecular biology to describe the similarity between the nucleotide or amino acid sequences of two or more genes or proteins. It is a measure of the degree to which the sequences are related, indicating a common evolutionary origin.

In other words, sequence homology implies that the compared sequences have a significant number of identical or similar residues in the same order, suggesting that they share a common ancestor and have diverged over time through processes such as mutation, insertion, deletion, or rearrangement. The higher the degree of sequence homology, the more closely related the sequences are likely to be.

Sequence homology is often used to identify similarities between genes or proteins from different species, which can provide valuable insights into their functions, structures, and evolutionary relationships. It is commonly assessed using various bioinformatics tools and algorithms, such as BLAST (Basic Local Alignment Search Tool), Clustal Omega, and multiple sequence alignment (MSA) methods.

A catalytic domain is a portion or region within a protein that contains the active site, where the chemical reactions necessary for the protein's function are carried out. This domain is responsible for the catalysis of biological reactions, hence the name "catalytic domain." The catalytic domain is often composed of specific amino acid residues that come together to form the active site, creating a unique three-dimensional structure that enables the protein to perform its specific function.

In enzymes, for example, the catalytic domain contains the residues that bind and convert substrates into products through chemical reactions. In receptors, the catalytic domain may be involved in signal transduction or other regulatory functions. Understanding the structure and function of catalytic domains is crucial to understanding the mechanisms of protein function and can provide valuable insights for drug design and therapeutic interventions.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Maltose is a disaccharide made up of two glucose molecules joined by an alpha-1,4 glycosidic bond. It is commonly found in malted barley and is created during the germination process when amylase breaks down starches into simpler sugars. Maltose is less sweet than sucrose (table sugar) and is broken down into glucose by the enzyme maltase during digestion.

GTP (Guanosine Triphosphate) Phosphohydrolase-Linked Elongation Factors are a group of proteins that play a crucial role in protein synthesis, specifically in the elongation phase of translation. These factors use the energy released from GTP hydrolysis to facilitate various steps in the addition of amino acids to the growing polypeptide chain during protein synthesis.

In prokaryotic cells, there are two main GTP Phosphohydrolase-Linked Elongation Factors: EF-Tu (Elongation Factor Thermos unstable) and EF-G (Elongation Factor G).

EF-Tu forms a complex with aminoacyl-tRNA and GTP, which then binds to the ribosome. Upon correct codon-anticodon recognition, GTP is hydrolyzed to GDP, releasing EF-Tu from the ribosome and allowing for the addition of the amino acid to the polypeptide chain.

EF-G, on the other hand, facilitates the translocation of the peptidyl-tRNA from the A site to the P site of the ribosome after peptide bond formation, using GTP hydrolysis as an energy source. This movement makes room for a new aminoacyl-tRNA to bind and continue the elongation process.

In eukaryotic cells, there are functionally equivalent factors called EF1A (eEF1A) and EF2 (eEF2), which perform similar roles in protein synthesis.

DNA topoisomerases are enzymes that modify the topological structure of DNA by regulating the number of twists or supercoils in the double helix. There are two main types of DNA topoisomerases: type I and type II.

Type I DNA topoisomerases function by cutting one strand of the DNA duplex, allowing the uncut strand to rotate around the break, and then resealing the break. This process can relieve both positive and negative supercoiling in DNA, as well as introduce single-stranded breaks into the DNA molecule.

Type I topoisomerases are further divided into three subtypes: type IA, type IB, and type IC. These subtypes differ in their mechanism of action and the structure of the active site tyrosine residue that makes the transient break in the DNA strand.

Overall, DNA topoisomerases play a crucial role in many cellular processes involving DNA, including replication, transcription, recombination, and chromosome segregation. Dysregulation of these enzymes has been implicated in various human diseases, including cancer and genetic disorders.

Minichromosome Maintenance 1 Protein (MCM1) is a protein that belongs to the minichromosome maintenance proteins complex, which is essential for the initiation and regulation of eukaryotic DNA replication. MCM1 is a crucial component of this complex, and it functions as a transcription factor that regulates the expression of genes involved in various cellular processes such as cell cycle progression, DNA repair, and development. In addition to its role in DNA replication and gene regulation, MCM1 has also been implicated in the development of certain types of cancer, making it an important area of research in cancer biology.

Peptide Elongation Factor 1 (PEF1) is not a commonly used medical term, but it is a term used in biochemistry and molecular biology. Here's the definition:

Peptide Elongation Factor 1 (also known as EF-Tu in prokaryotes or EFT1A/EFT1B in eukaryotes) is a protein involved in the elongation phase of protein synthesis, specifically during translation. It plays a crucial role in delivering aminoacyl-tRNAs to the ribosome, enabling the addition of new amino acids to the growing polypeptide chain.

In eukaryotic cells, EF1A and EF1B (also known as EF-Ts) form a complex that helps facilitate the binding of aminoacyl-tRNAs to the ribosome. In prokaryotic cells, EF-Tu forms a complex with GTP and aminoacyl-tRNA, which then binds to the ribosome. Once bound, GTP is hydrolyzed to GDP, causing a conformational change that releases the aminoacyl-tRNA into the acceptor site of the ribosome, allowing for peptide bond formation. The EF-Tu/GDP complex then dissociates from the ribosome and is recycled by another protein called EF-G (EF-G in prokaryotes or EFL1 in eukaryotes).

Therefore, Peptide Elongation Factor 1 plays a critical role in ensuring that the correct amino acids are added to the growing peptide chain during protein synthesis.

Alcohol dehydrogenase (ADH) is a group of enzymes responsible for catalyzing the oxidation of alcohols to aldehydes or ketones, and reducing equivalents such as NAD+ to NADH. In humans, ADH plays a crucial role in the metabolism of ethanol, converting it into acetaldehyde, which is then further metabolized by aldehyde dehydrogenase (ALDH) into acetate. This process helps to detoxify and eliminate ethanol from the body. Additionally, ADH enzymes are also involved in the metabolism of other alcohols, such as methanol and ethylene glycol, which can be toxic if allowed to accumulate in the body.

A replication origin is a specific location in a DNA molecule where the process of DNA replication is initiated. It serves as the starting point for the synthesis of new strands of DNA during cell division. The origin of replication contains regulatory elements and sequences that are recognized by proteins, which then recruit and assemble the necessary enzymes to start the replication process. In eukaryotic cells, replication origins are often found in clusters, with multiple origins scattered throughout each chromosome.

Adenosine Triphosphate (ATP) is a high-energy molecule that stores and transports energy within cells. It is the main source of energy for most cellular processes, including muscle contraction, nerve impulse transmission, and protein synthesis. ATP is composed of a base (adenine), a sugar (ribose), and three phosphate groups. The bonds between these phosphate groups contain a significant amount of energy, which can be released when the bond between the second and third phosphate group is broken, resulting in the formation of adenosine diphosphate (ADP) and inorganic phosphate. This process is known as hydrolysis and can be catalyzed by various enzymes to drive a wide range of cellular functions. ATP can also be regenerated from ADP through various metabolic pathways, such as oxidative phosphorylation or substrate-level phosphorylation, allowing for the continuous supply of energy to cells.

Deoxyguanosine is a chemical compound that is a component of DNA (deoxyribonucleic acid), one of the nucleic acids. It is a nucleoside, which is a molecule consisting of a sugar (in this case, deoxyribose) and a nitrogenous base (in this case, guanine). Deoxyguanosine plays a crucial role in the structure and function of DNA, as it pairs with deoxycytidine through hydrogen bonding to form a rung in the DNA double helix. It is involved in the storage and transmission of genetic information.

Nucleotides are the basic structural units of nucleic acids, such as DNA and RNA. They consist of a nitrogenous base (adenine, guanine, cytosine, thymine or uracil), a pentose sugar (ribose in RNA and deoxyribose in DNA) and one to three phosphate groups. Nucleotides are linked together by phosphodiester bonds between the sugar of one nucleotide and the phosphate group of another, forming long chains known as polynucleotides. The sequence of these nucleotides determines the genetic information carried in DNA and RNA, which is essential for the functioning, reproduction and survival of all living organisms.

"Pyrococcus furiosus" is not a medical term, but a scientific name for an extremophilic archaea species. It's a type of microorganism that thrives in extreme environments, particularly high temperature and acidity. "Pyrococcus furiosus" was first isolated from a marine volcanic vent and has since been studied extensively due to its unique biological properties.

In terms of scientific definition:

"Pyrococcus furiosus" is a species of archaea belonging to the order Thermococcales, family Pyrococcaceae. It's a hyperthermophilic organism, with an optimum growth temperature of around 100°C (212°F), and can survive in temperatures up to 106°C (223°F). The cells are irregularly coccoid, about 0.8-1.5 µm in diameter, and occur singly or in pairs.

The organism obtains energy by fermenting peptides and carbohydrates, producing hydrogen, carbon dioxide, and acetate as end products. "Pyrococcus furiosus" has been used as a model system for studying the biochemistry of archaea and extremophiles, including enzymes that function optimally at high temperatures.

X-ray emission spectrometry is a technique used to analyze the elements present in a sample by measuring the characteristic X-rays that are emitted when the sample is bombarded with high-energy X-rays or charged particles. The sample is excited to emit X-rays, which have specific energies (wavelengths) that correspond to the energy levels of the electrons in the atoms of the elements present in the sample. These X-ray emissions are then detected and analyzed using a spectrometer, which separates and measures the intensity of the different X-ray energies. The resulting spectrum provides information about the identity and quantity of the elements present in the sample. This technique is widely used in materials analysis, particularly for the identification and quantification of heavy metals and other elements in a variety of samples, including geological, biological, and industrial materials.

Gel chromatography is a type of liquid chromatography that separates molecules based on their size or molecular weight. It uses a stationary phase that consists of a gel matrix made up of cross-linked polymers, such as dextran, agarose, or polyacrylamide. The gel matrix contains pores of various sizes, which allow smaller molecules to penetrate deeper into the matrix while larger molecules are excluded.

In gel chromatography, a mixture of molecules is loaded onto the top of the gel column and eluted with a solvent that moves down the column by gravity or pressure. As the sample components move down the column, they interact with the gel matrix and get separated based on their size. Smaller molecules can enter the pores of the gel and take longer to elute, while larger molecules are excluded from the pores and elute more quickly.

Gel chromatography is commonly used to separate and purify proteins, nucleic acids, and other biomolecules based on their size and molecular weight. It is also used in the analysis of polymers, colloids, and other materials with a wide range of applications in chemistry, biology, and medicine.

Electron Transport Complex III, also known as cytochrome bc1 complex or ubiquinol-cytochrome c reductase, is a protein complex located in the inner mitochondrial membrane of eukaryotic cells and the cytoplasmic membrane of prokaryotic cells. It plays a crucial role in the electron transport chain (ETC), a series of complexes that generate energy in the form of ATP through a process called oxidative phosphorylation.

In ETC, Electron Transport Complex III accepts electrons from ubiquinol and transfers them to cytochrome c. This electron transfer is coupled with the translocation of protons (H+ ions) across the membrane, creating an electrochemical gradient. The energy stored in this gradient drives the synthesis of ATP by ATP synthase.

Electron Transport Complex III consists of several subunits, including cytochrome b, cytochrome c1, and the Rieske iron-sulfur protein. These subunits work together to facilitate the electron transfer and proton translocation processes.

A protein subunit refers to a distinct and independently folding polypeptide chain that makes up a larger protein complex. Proteins are often composed of multiple subunits, which can be identical or different, that come together to form the functional unit of the protein. These subunits can interact with each other through non-covalent interactions such as hydrogen bonds, ionic bonds, and van der Waals forces, as well as covalent bonds like disulfide bridges. The arrangement and interaction of these subunits contribute to the overall structure and function of the protein.

"Methanococcus" is a genus of archaea, which are single-celled microorganisms that share some characteristics with bacteria but are actually more closely related to eukaryotes. "Methanococcus" species are obligate anaerobes, meaning they can only survive in environments without oxygen. They are also methanogens, which means they produce methane as a byproduct of their metabolism. These microorganisms are commonly found in aquatic environments such as marine sediments and freshwater swamps, where they play an important role in the carbon cycle by breaking down organic matter and producing methane. Some "Methanococcus" species can also be found in the digestive tracts of animals, including humans, where they help to break down food waste and produce methane as a byproduct.

An operon is a genetic unit in prokaryotic organisms (like bacteria) consisting of a cluster of genes that are transcribed together as a single mRNA molecule, which then undergoes translation to produce multiple proteins. This genetic organization allows for the coordinated regulation of genes that are involved in the same metabolic pathway or functional process. The unit typically includes promoter and operator regions that control the transcription of the operon, as well as structural genes encoding the proteins. Operons were first discovered in bacteria, but similar genetic organizations have been found in some eukaryotic organisms, such as yeast.

Succinate dehydrogenase (SDH) is an enzyme complex that plays a crucial role in the process of cellular respiration, specifically in the citric acid cycle (also known as the Krebs cycle) and the electron transport chain. It is located in the inner mitochondrial membrane of eukaryotic cells.

SDH catalyzes the oxidation of succinate to fumarate, converting it into a molecule of fadaquate in the process. During this reaction, two electrons are transferred from succinate to the FAD cofactor within the SDH enzyme complex, reducing it to FADH2. These electrons are then passed on to ubiquinone (CoQ), which is a mobile electron carrier in the electron transport chain, leading to the generation of ATP, the main energy currency of the cell.

SDH is also known as mitochondrial complex II because it is the second complex in the electron transport chain. Mutations in the genes encoding SDH subunits or associated proteins have been linked to various human diseases, including hereditary paragangliomas, pheochromocytomas, gastrointestinal stromal tumors (GISTs), and some forms of neurodegenerative disorders.

DNA adducts are chemical modifications or alterations that occur when DNA molecules become attached to or bound with certain harmful substances, such as toxic chemicals or carcinogens. These attachments can disrupt the normal structure and function of the DNA, potentially leading to mutations, genetic damage, and an increased risk of cancer and other diseases.

DNA adducts are formed when a reactive molecule from a chemical agent binds covalently to a base in the DNA molecule. This process can occur either spontaneously or as a result of exposure to environmental toxins, such as those found in tobacco smoke, certain industrial chemicals, and some medications.

The formation of DNA adducts is often used as a biomarker for exposure to harmful substances, as well as an indicator of potential health risks associated with that exposure. Researchers can measure the levels of specific DNA adducts in biological samples, such as blood or urine, to assess the extent and duration of exposure to certain chemicals or toxins.

It's important to note that not all DNA adducts are necessarily harmful, and some may even play a role in normal cellular processes. However, high levels of certain DNA adducts have been linked to an increased risk of cancer and other diseases, making them a focus of ongoing research and investigation.

PubMed references for Sulfolobus PubMed Central references for Sulfolobus Google Scholar references for Sulfolobus NCBI ... taxonomy pages for Sulfolobus Search Species2000 page for Sulfolobus MicrobeWiki page for Sulfolobus LPSN page for Sulfolobus ... Sulfolobus is a genus of microorganism in the family Sulfolobaceae. It belongs to the archaea domain. Sulfolobus species grow ... Species of Sulfolobus are generally named after the location from which they were first isolated, e.g. Sulfolobus solfataricus ...
These are small and have been found in several strains of Sulfolobus but not in other genome. Chromatin protein in Sulfolobus ... has since made Sulfolobus an ideal model system for transcription studies. Recent studies in Sulfolobus, in addition to other ... and reclassification of Sulfolobus solfataricus as Saccharolobus solfataricus comb. nov. and Sulfolobus shibatae as ... The genome of Sulfolobus is characterised by the presence of short tandem repeats, insertion and repetitive elements, it has a ...
This Sulfolobus species grows on a limited range of carbon sources, relative to other Sulfolobus species, and this might be due ... Sulfolobus acidocaldarius possess a mechanism of replication homologous to the eukaryotic ESCRT. Sulfolobus acidocaldarius is a ... The genome of Sulfolobus acidocaldarius is very stable, with little, if any, rearrangements due to mobile elements.[citation ... The springs where this species was isolated had a pH less than 3 and temperatures in the range of 65-90 °C. Sulfolobus ...
"Sulfolobus tokodaii sp. nov. (f. Sulfolobus sp. strain 7), a new member of the genus Sulfolobus isolated from Beppu Hot Springs ... "Sulfolobus tokodaii" at the Encyclopedia of Life LPSN Type strain of Sulfolobus tokodaii at BacDive - the Bacterial Diversity ... Sulfolobus tokodaii is a thermophilic archaeon. It is acidophilic and obligately aerobic. The type strain is 7 (JCM 10545). Its ... 2001). "Complete genome sequence of an aerobic thermoacidophilic crenarchaeon, Sulfolobus tokodaii strain7". DNA Res. 8 (4): ...
2002). "Sulfolobus tokodaii sp. nov. (f. Sulfolobus sp. strain 7), a new member of the genus Sulfolobus isolated from Beppu Hot ... is a close relative to Sulfolobus metallicus with comparable phylogenetic properties. Both Sulfolobus metallicus and Sulfolobus ... Sulfolobus metallicus can also oxidize iron(II). Sulfolobus metallicus has a unique type II NADH dehydrogenase with no iron- ... Sulfolobus metallicus can potentially be used to provide a cheaper way to synthesize these lipids. If Sulfolobus metallicus is ...
... (SIFV) is an archaeal virus, classified in the family Lipothrixviridae within the order ... The virus infects hypethermophilic and acidophilic archaeon Sulfolobus islandicus. SIFV has a linear double-stranded DNA genome ... 2000). "A novel lipothrixvirus, SIFV, of the extremely thermophilic crenarchaeon Sulfolobus". Virology. 267 (2): 252-266. doi: ...
... 1 Sulfolobus islandicus rod-shaped virus 2 This disambiguation page lists articles about ... Sulfolobus islandicus rod-shaped virus refers to two different species of virus, both members of the genus Rudivirus: ...
... (formerly Sulfolobus turreted icosahedral virus) is a species of virus that infects the ... "Atomic structure of the 75 MDa extremophile Sulfolobus turreted icosahedral virus determined by CryoEM and X-ray ... archaeon Sulfolobus solfataricus. This virus was isolated from a hot spring in the Rabbit Creek thermal area which is located ...
UCSC Sulfolobus virus STSV1 Genome Browser Gateway ENA Genomes Pages - Archaealvirus STSV-1, also STSV-2, and Sulfolobus ... "A novel single-tailed fusiform Sulfolobus virus STSV2 infecting model Sulfolobus species". Extremophiles: Life Under Extreme ... Sulfolobus tengchongensis spindle-shaped virus 1 (STSV1) is a DNA virus of the family Bicaudaviridae. It infects the ... In 2014, Sulfolobus tengchongensis spindle-shaped virus 2 (STSV2), a relative of STSV1, also infecting S. tengchongensis, has ...
"Sulfolobus tokodaii sp. nov. (f. Sulfolobus sp. strain 7), a new member of the genus Sulfolobus isolated from Beppu Hot Springs ... "Sulfolobus tokodaii - microbewiki". microbewiki.kenyon.edu. Retrieved 2021-11-20. Suzuki, Toshiharu; Iwasaki, Toshio; Uzawa, ... Kawarabayasi, Y. (2001-01-01). "Complete Genome Sequence of an Aerobic Thermoacidophilic Crenarchaeon, Sulfolobus tokodaii ...
Originally classified as a member of the genus Sulfolobus, Kurosawa et al. determined through genetic testing that the organism ... determined a 92% similarity with Sulfolobus species; however, Kurosawa et al. determined a 98% similarity with Metallosphaera ... Kurosawa, Norio; Itoh, Yuko H.; Itoh, Takashi (2003). "Reclassification of Sulfolobus hakonensis Takayanagi et al. 1996 as ... a media known to sustain Sulfolobus species, was made and incubated at 70 °C for about one week. This sample was then used to ...
Schäfer, Günter (December 1996). "Bioenergetics of the archaebacterium Sulfolobus". Biochimica et Biophysica Acta (BBA) - ... "The complete genome of the crenarchaeon Sulfolobus solfataricus P2". Proceedings of the National Academy of Sciences. 98 (14): ... deficiency of chromatin proteins is a non-mutational and epigenetic-like trait in evolved lines of the archaeon Sulfolobus ...
Sulfolobus ellipsoid virus 1 was isolated from an acidic hot spring (86−106oC, pH 2.2−2.5) in Laguna Fumarólica, Costa Rica; ... The family contains a single genus, Alphaovalivirus, which contains a single species, Sulfolobus ellipsoid virus 1. The linear ... "Genome Sequencing of Sulfolobus sp. A20 from Costa Rica and Comparative Analyses of the Putative Pathways of Carbon, Nitrogen, ... the only known host is Sulfolobus sp. A20. Huang, L; Wang, H; ICTV Report Consortium (2020-12-17). "ICTV Virus Taxonomy Profile ...
Sulfolobus islandicus rod-shaped virus 1 (SIRV1) is a virus in the order Ligamenvirales. Its only known host is the Archaean ... "Sulfolobus islandicus rod-shaped virus 1". GenomeNet. GenomeNet. Retrieved January 7, 2019. Bautista, Maria A.; Black, Jesse A ... Youngblut, Nicholas D.; Whitaker, Rachel J. (2017). "Differentiation and Structure in Sulfolobus islandicus Rod-Shaped Virus ... Sulfolobus islandicus. The species was first documented from a hot spring sample in Yellowstone National Park. "ICTV Taxonomy ...
Sulfolobus newzealandicus serve as natural hosts. There is only one species in this genus: Sulfolobus newzealandicus droplet- ... Sulfolobus newzealandicus serve as the natural host. Prangishvili, D; Mochizuki, T; Krupovic, M; ICTV Report Consortium (8 ...
Evguenieva-Hackenberg, E; Walter, P; Hochleitner, E; Lottspeich, F; Klug, G (2003). "An exosome-like complex in Sulfolobus ... "Characterization of native and reconstituted exosome complexes from the hyperthermophilic archaeon Sulfolobus solfataricus". ...
Reno ML, Held NL, Fields CJ, Burke PV, Whitaker RJ (May 2009). "Biogeography of the Sulfolobus islandicus pan-genome". ... April 2011). "Genome analyses of Icelandic strains of Sulfolobus islandicus, model organisms for genetic and virus-host ... July 2001). "The complete genome of the crenarchaeon Sulfolobus solfataricus P2". Proceedings of the National Academy of ... July 2005). "The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota". Journal of Bacteriology. 187 (14 ...
Sulfolobus plasmids pSSVi and pSSVx not only show relation to fuselloviruses but act as satellites of them and can be ... Sulfolobus islandicus rod-shaped virus 2 (SIRV2) attaches to pili and then moves along the pili toward the cell. Caudoviruses ... Sulfolobus spindle-shaped virus 1 (SSV1), SIRV2, and STIV have been developed into model systems to study virus-host ... Sulfolobus turreted icosahedral virus 1 (STIV1) and SIRV2 exit cells through pyramidal structures formed on the surface of ...
The archaea Sulfolobus solfataricus serve as natural hosts. There are two species in the genus Alphaturrivirus. The genus ... Sulfolobus solfataricus serves as the natural host. Transmission routes are passive diffusion. "Viral Zone". ExPASy. Retrieved ... contains the following species: Sulfolobus turreted icosahedral virus 1 Viruses in Turriviridae have icosahedral geometries, ...
June 2007). "Flagellar motility and structure in the hyperthermoacidophilic archaeon Sulfolobus solfataricus". Journal of ... "Appendage-mediated surface adherence of Sulfolobus solfataricus". Journal of Bacteriology. 192 (1): 104-10. doi:10.1128/JB. ...
Archaea in the genus Sulfolobus use caldariellaquinone. The use of different quinones is due to slight changes in redox ...
Reno ML, Held NL, Fields CJ, Burke PV, Whitaker RJ (May 2009). "Biogeography of the Sulfolobus islandicus pan-genome". ...
Protein L-isoaspartyl-O-methyltransferase from Sulfolobus tokodaii". The Journal of Biological Chemistry. 279 (31): 32957-32967 ...
Sulfolobus solfataricus and Sulfolobus acidocaldarius are hyperthermophilic archaea. Exposure of these organisms to the DNA ... It has also been suggested that DNA transfer in Sulfolobus may be an early form of sexual interaction similar to the more well- ... hypothesized that cellular aggregation enhances species-specific DNA transfer between Sulfolobus cells in order to repair ... November 2008). "UV-inducible cellular aggregation of the hyperthermophilic archaeon Sulfolobus solfataricus is mediated by ...
... and reclassification of Sulfolobus solfataricus as Saccharolobus solfataricus comb. nov. and Sulfolobus shibatae as ... represents a new species of the archaebacterial genus Sulfolobus, Sulfolobus shibatae, sp. nov". Archives of Microbiology. 154 ... Type strain of Sulfolobus shibatae at BacDive - the Bacterial Diversity Metadatabase (Articles with short description, Short ... It was transferred from the genus Sulfolobus to the new genus Saccharolobus with the description of Saccharolobus caldissimus ...
doi:10.1016/0168-1656(94)90093-0. Brock TD (1981). "Extreme Thermophiles of the Genera Thermus and Sulfolobus". The Prokaryotes ...
Sulfolobus solfataricus and Sulfolobus acidocaldarius are hyperthermophilic archaea. When these organisms are exposed to the ... Also it has been suggested that DNA transfer in Sulfolobus may be a primitive form of sexual interaction similar to the more ... Fröls S; White MF; Schleper C (February 2009). "Reactions to UV damage in the model archaeon Sulfolobus solfataricus". Biochem ... and Ajon et al.(2011) hypothesized that cellular aggregation enhances species-specific DNA transfer between Sulfolobus cells in ...
In Sulfolobus solfataricus, for example, three chromosomal origins have been mapped (oriC1, oriC2, and oriC3), and biochemical ... Lundgren M, Andersson A, Chen L, Nilsson P, Bernander R (May 2004). "Three replication origins in Sulfolobus species: ... has been shown to bind all origins as well and to drive origin activity of oriC3 in the closely related Sulfolobus islandicus. ... "Identification of two origins of replication in the single chromosome of the archaeon Sulfolobus solfataricus". Cell. 116 (1): ...
Sulfolobus acidocaldarius has been observed forming tower-like biofilm structures and Sulfolobus solfataricus has been observed ... islandicus and certain other Sulfolobus species. Other species, such as Sulfolobus acidocaldarius, are not inhibited. The gene ... Unique to Sulfolobus acidocaldarious are the archaeal adhesive pili which are important for surface attachment in biofilm ... A sugar-binding surface structure termed bindosome has been found in Sulfolobus solfataricus. When assembled into a dedicated ...
1991 Sulfodiicoccus Sakai & Kurosawa 2017 Sulfolobus Brock et al. 1972 Sulfuracidifex Itoh et al. 2020 Sulfurisphaera Kurosawa ...
PubMed references for Sulfolobus PubMed Central references for Sulfolobus Google Scholar references for Sulfolobus NCBI ... taxonomy pages for Sulfolobus Search Species2000 page for Sulfolobus MicrobeWiki page for Sulfolobus LPSN page for Sulfolobus ... Sulfolobus is a genus of microorganism in the family Sulfolobaceae. It belongs to the archaea domain. Sulfolobus species grow ... Species of Sulfolobus are generally named after the location from which they were first isolated, e.g. Sulfolobus solfataricus ...
Structure of the RNAse SSO8090 from Sulfolobus solfataricus ... Structure of the RNAse SSO8090 from Sulfolobus solfataricus. * ... Structure of the RNAse SSO8090 from Sulfolobus solfataricus. Proudfoot, M., Brown, M., Singer, A.U., Skarina, T., Tan, K., ...
Sulfolobus is a sulfate-reducer that uses sulfur as an energy source and converts it into sulfuric acid. ... Sulfolobus solfataricus was originally isolated from the Sulfatara hot springs in Italy. It is a mobile thermoacidophile ... Find out more about this interesting microbe here: https://joidesresolution.org//microbe-monday-sulfolobus-solfataricus/ ...
Timeline for Species Sulfolobus solfataricus [TaxId:2287] from d.273.1.1 Hypothetical protein SSO2532: *Species Sulfolobus ... Lineage for Species: Sulfolobus solfataricus. *Root: SCOP 1.71 *. Class d: Alpha and beta proteins (a+b) [53931] (286 folds). ... PDB entry in Species: Sulfolobus solfataricus:. *Domain(s) for 1vph: *. Domain d1vpha_: 1vph A: [113955]. ... Species Sulfolobus solfataricus [TaxId:2287] from d.273.1.1 Hypothetical protein SSO2532 appears in SCOP 1.73. *Species ...
Timeline for Species Sulfolobus acidocaldarius [TaxId:2285] from g.41.7.1 Aspartate carbamoyltransferase, Regulatory-chain, C- ... PDB entries in Species: Sulfolobus acidocaldarius [TaxId: 2285]:. *Domain(s) for 1pg5: *. Domain d1pg5b2: 1pg5 B:105-160 [ ... Lineage for Species: Sulfolobus acidocaldarius [TaxId: 2285]. *Root: SCOPe 2.08 *. Class g: Small proteins [56992] (100 folds) ... Species Sulfolobus acidocaldarius [TaxId:2285] from g.41.7.1 Aspartate carbamoyltransferase, Regulatory-chain, C-terminal ...
The combination of a RT-PCR strategy with shotgun proteomics demonstrates that interrupted genes in the archaeon Sulfolobus ...
Sulfolobus solfataricus uracil phosphoribosyltransferase in complex with uridine 5-monophosphate (UMP) ... The UPRTase from Sulfolobus solfataricus has a unique regulation by nucleoside triphosphates compared to UPRTases from other ... The UPRTase from Sulfolobus solfataricus has a unique regulation by nucleoside triphosphates compared to UPRTases from other ... Allosteric Regulation and Communication between Subunits in Uracil Phosphoribosyltransferase from Sulfolobus solfataricus(,). ...
Sulfolobus islandicus L.S.2.15). Find diseases associated with this biological target and compounds tested against it in ...
The Indolglycerinphosphate-synthase of Sulfolobus solfataricus (sTrpC) is a well characterized enzyme with a (βα)8-barrel fold ... The Indolglycerinphosphate-synthase of Sulfolobus solfataricus (sTrpC) is a well characterized enzyme with a (βα)8-barrel fold ... Die Indolglycerinphosphat-Synthase aus Sulfolobus solfataricus (sTrpC) ist ein gut charakterisiertes Enzym mit einer (βα)8- ... Die Indolglycerinphosphat-Synthase aus Sulfolobus solfataricus (sTrpC) ist ein gut charakterisiertes Enzym mit einer (βα)8- ...
The structural basis of substrate promiscuity in glucose dehydrogenase from the hyperthermophilic archaeon Sulfolobus ...
Sulfolobus islandicus. Sis Kingdom:. Archaeon. Links:. at NCBI at Uniprot Polymerases:. Polymerase. Family. Reference count. ... Information about Sulfolobus islandicus (Sis) from Archaeon ...
In publishing the research results obtained by use of the BIOLOGICAL RESOURCE, the USER is expected to cite the literature specified by the DEPOSITOR ...
Sulfolobus tokodaii - STS059. Organism. Sulfolobus tokodaii. Gene Name. STS059. Product. 30S ribosomal protein S14. ...
Illustrated evolutionary lineage of Sulfolobus Brock & al. 1972. ...
Sulfolobus solfataricus protein disulphide oxidoreductase: insight into the roles of its redox sites (249 views). Protein ... The Crystal Structure Of Sulfolobus Solfataricus Elongation Factor 1 Alpha In Complex With Magnesium And Gdp (506 views). ... Structural study of a single-point mutant of Sulfolobus solfataricus alcohol dehydrogenase with enhanced activity (331 views). ... Sulfolobus solfataricus thiol redox puzzle: characterization of an atypical protein disulfide oxidoreductase (460 views). ...
Several Sulfolobus shuttle vector systems are available and since 2007 also for Sulfolobus acidocaldarius. SSO1949 was ... nämlich in dem Crenarchaeot Sulfolobus. Seit 2007 steht für Sulfolobus acidocaldarius ein Shuttle-Vektor-System zur Verfügung, ... The genus Sulfolobus is one of the best studied archaeal organisms and it offers appropriate genetic systems for expression of ... Sulfolobus; Thermotoga; Cellulasen; Shuttle-Vektor; Rückfaltung; hybrid protein; cellulase; shuttle vector. DDC Subjects:. 500 ...
... MORACCI, Marco;Trincone, Antonio ... Enzymatic synthesis of oligosaccharides by two glycosyl hydrolases of Sulfolobus solfataricus / Moracci, Marco; Trincone, ... Enzymatic synthesis of oligosaccharides by two glycosyl hydrolases of Sulfolobus solfataricus / Moracci, Marco; Trincone, ... philic archaeon Sulfolobus solfataricus are briefly reviewed. The approaches used and the biodiversity of the catalysts ...
... from the archaeon Sulfolobus solfataricus was purified from the supernatant of acid-soluble cell lysates. Reverse phase HPLC of ... The thermostable histone-like protein Sso7c (Sso for Sulfolobus solfataricus) from the archaeon Sulfolobus solfataricus was ... Isolation and structure of repressor-like proteins from the archaeon Sulfolobus solfataricus. Co-purification of RNase A with ... Isolation and structure of repressor-like proteins from the archaeon Sulfolobus solfataricus. Co-purification of RNase A with ...
... RAIMO, Gennaro; ... EF-2 and EF-1β isolated from the hyperthermophilic archaeon Sulfolobus solfataricus. During the elongation cycle the GTPase ... EF-2 and EF-1β isolated from the hyperthermophilic archaeon Sulfolobus solfataricus. During the elongation cycle the GTPase ...
Three-dimensional electron microscopy of the reverse gyrase from Sulfolobus tokodaii. Kyoko Matoba, Kouta Mayanagi, Syo Nakasu ... Three-dimensional electron microscopy of the reverse gyrase from Sulfolobus tokodaii. / Matoba, Kyoko; Mayanagi, Kouta; Nakasu ... Three-dimensional electron microscopy of the reverse gyrase from Sulfolobus tokodaii. In: Biochemical and Biophysical Research ... Electron microscopy combined with single particle analyses revealed the three-dimensional structure of the DNA-free Sulfolobus ...
... RAIMO G.;ARCARI P.; ... philic archaeon Sulfolobus solfataricus. During the elongation cycle the GTPase activity of SsEF-1α and SsEF-2 and the ... philic archaeon Sulfolobus solfataricus. During the elongation cycle the GTPase activity of SsEF-1α and SsEF-2 and the ...
SULFOLOBUS SOLFATARICUS TRYPTOPHAN SYNTHASE B2O - 6EQN , canSARS ... SULFOLOBUS SOLFATARICUS. --. Mutations 6EQN_D Q97TX6 TRPB2, ...
5-D(*CP*CP*TP*AP*TP*AP*TP*AP*GP*G)-3DNA-BINDING PROTEINS 7A/7B/7D
... found in Sulfolobus acidocaldarius and several other members of the Sulfolobales, a branch of the Crenarchaeota ... WP_010923978 10 SIKRKSKYTLGVLLLASFLAIIMGLANVPMAQTSPQIPVYKVVGNADLSNPGSASYWSQIPWINISLTANIPMAPTSGLT 89 Sulfolobus solf... WP_ ... WP_010923978 90 HYLLVKAVWNGSWIIILERWYAPEPAFGAWSAAAAALYPPASGPGLFRQIMLTPGTTYTIEKNYTNYFSIVNGNIIQGRL 169 Sulfolobus solf... WP_ ... WP_010923978 170 VLNYSGILLPAPNDTQITVLSNGTIILWHSPRPIEDLLYSDGMFYGYYTNNTWYYPDRAAIMWYMGSVIPpTKDGMNIGG 249 Sulfolobus solf... WP_ ...
Attack from both ends: mRNA degradation in the crenarchaeon Sulfolobus solfataricus Elena Evguenieva-Hackenberg; Elena ... Elena Evguenieva-Hackenberg, Udo Bläsi; Attack from both ends: mRNA degradation in the crenarchaeon Sulfolobus solfataricus. ... directional decay in the crenarchaeon Sulfolobus solfataricus, which is executed by a RNase J-like ribonuclease and the exosome ...
Sulfolobus acidocaldarius 5yeq_a Q4J8K9 99.60 1.20E-19 7.10E-24 153.80 0 0 0 0 0 0 0 0 ...
The crystal structure of a-glucosidase MalA from Sulfolobus solfataricus has been determined at 2.5 Å resolution. It provides a ... Structure of the Sulfolobus solfataricus alpha-glucosidase: Implications for domain conservation and substrate recognition in ...
... ... Sulfolobus solfataricus protein disulphide oxidoreductase: insight into the roles of its redox sites (240 views). Protein ... Biochemical Characterisation Of The D60a Mutant Of The Elongation Factor 1 Alpha From The Archaeon Sulfolobus Solfataricus. No ... Structural and functional studies of Stf76 from the Sulfolobus islandicus plasmid-virus pSSVx: a novel peculiar member of the ...
  • Sulfolobus solfataricus was first isolated in the Solfatara volcano. (wikipedia.org)
  • In 2004, the origins of DNA replication of Sulfolobus solfataricus and Sulfolobus acidocaldarius were identified. (wikipedia.org)
  • The archaeon Sulfolobus solfataricus has a circular chromosome that consists of 2,992,245 bp. (wikipedia.org)
  • Sulfolobus solfataricus was originally isolated from the Sulfatara hot springs in Italy. (joidesresolution.org)
  • The combination of a RT-PCR strategy with shotgun proteomics demonstrates that interrupted genes in the archaeon Sulfolobus solfataricus are expressed in vivo. (nih.gov)
  • Die Indolglycerinphosphat-Synthase aus Sulfolobus solfataricus (sTrpC) ist ein gut charakterisiertes Enzym mit einer (βα)8-barrel Struktur, das den vierten Schritt der Tryptophanbiosynthese katalysiert. (uni-regensburg.de)
  • We report on the characterization of SsPDO, isolated from the hyperthermophilic archaeon Sulfolobus solfataricus. (cnr.it)
  • Als selektive Marker für die Uracil-Selektion dienten die funktionsfähigen pyrEF-Gene aus Sulfolobus solfataricus P2, welche für Enzyme des Uridinmonophosphat-Syntheseweges codieren. (uni-bayreuth.de)
  • SSO1949 zeigt 85% Sequenzidentität zu einer weiteren Endoglukanase aus Sulfolobus solfataricus. (uni-bayreuth.de)
  • Here, two methods of oligosaccharide synthesis performed by a glyco- synthase and by an α-xylosidase from the hyperthermo- philic archaeon Sulfolobus solfataricus are briefly reviewed. (unina.it)
  • Isolation and structure of repressor-like proteins from the archaeon Sulfolobus solfataricus. (ox.ac.uk)
  • The thermostable histone-like protein Sso7c (Sso for Sulfolobus solfataricus) from the archaeon Sulfolobus solfataricus was purified from the supernatant of acid-soluble cell lysates. (ox.ac.uk)
  • The present article reviews our recent work carried out on the translation elongation factors EF-1α, EF-2 and EF-1β isolated from the hyperthermophilic archaeon Sulfolobus solfataricus. (unimol.it)
  • In the present paper, we first briefly review the general mRNA decay pathways in Bacteria and Eukarya, and then focus on 5′-3′ and 3′-5′-directional decay in the crenarchaeon Sulfolobus solfataricus , which is executed by a RNase J-like ribonuclease and the exosome complex respectively. (silverchair.com)
  • The crystal structure of a-glucosidase MalA from Sulfolobus solfataricus has been determined at 2.5 Å resolution. (ku.dk)
  • The Catalytic Mechanism of Indole-3-Glycerol Phosphate Synthase: Crystal Structures of Complexes of the Enzyme From Sulfolobus Solfataricus with Substrate Analogue, Substrate, and Product. (atomistry.com)
  • 2.0 A structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability. (expasy.org)
  • Structural Basis for Error-Free Bypass of the 5-N-Methylformamidopyrimidine-dG Lesion by Human DNA Polymerase eta and Sulfolobus solfataricus P2 Polymerase IV. (cathdb.info)
  • Seit 2007 steht für Sulfolobus acidocaldarius ein Shuttle-Vektor-System zur Verfügung, in welchem SSO1949 unter Kontrolle verschiedener induzierbarer und konstitutiver Promotoren exprimiert wurde. (uni-bayreuth.de)
  • cytochrome b558/566, subunit A Members of this protein family are CbsA, one subunit of a highly glycosylated, heterodimeric, mono-heme cytochrome b558/566, found in Sulfolobus acidocaldarius and several other members of the Sulfolobales, a branch of the Crenarchaeota. (nih.gov)
  • YtrASa, a GntR-family transcription factor represses two genetic loci encoding membrane proteins in Sulfolobus acidocaldarius. (vub.be)
  • Desulfurisation of coal water mixtures using Sulfolobus acidocaldarius. (southwales.ac.uk)
  • Furthermore, fluctuation tests on a hyperthermophilic archeaon Sulfolobus acidocaldarius [ 6 ] and a hyperthermophilic bacterium Thermus thermophilus [ 7 ] consistently showed that hyperthermophiles have much lower mutation rate compared to mesophiles. (nature.com)
  • Sulfolobus islandicus, a microbe that can live in boiling acid, is offering up its secrets to researchers hardy enough to capture it from the volcanic hot springs where it thrives. (sciencedaily.com)
  • Electron microscopy combined with single particle analyses revealed the three-dimensional structure of the DNA-free Sulfolobus tokodaii reverse gyrase and two-dimensional average images of both the protein alone and that complexed with double-stranded DNA. (elsevierpure.com)
  • Sulfolobus species grow in volcanic springs with optimal growth occurring at pH 2-3 and temperatures of 75-80 °C, making them acidophiles and thermophiles respectively. (wikipedia.org)
  • Most of the genes that are coming and going, at least on Sulfolobus, seem to be on viruses and plasmids," Whitaker said. (sciencedaily.com)
  • The viruses and plasmids that had lent their genes to Sulfolobus in one site were different from those found in another. (sciencedaily.com)
  • Species of Sulfolobus are generally named after the location from which they were first isolated, e.g. (wikipedia.org)
  • Intracellular proteins are not necessarily stable at low pH however, as Sulfolobus species maintain a significant pH gradient across the outer membrane. (wikipedia.org)
  • The tetraethers help Sulfolobus species survive extreme acid as well as high temperature. (wikipedia.org)
  • Sulfolobus proteins are of interest for biotechnology and industrial use due to their thermostable nature. (wikipedia.org)
  • Since this step is important for an aerobic microorganism like Sulfolobus, it probably uses a different molecule for the same function or has a different pathway. (wikipedia.org)
  • Sulfolobus can grow either lithoautotrophically by oxidizing sulfur, or chemoheterotrophically using sulfur to oxidize simple reduced carbon compounds. (wikipedia.org)
  • Sulfolobus is a sulfate-reducer that uses sulfur as an energy source and converts it into sulfuric acid. (joidesresolution.org)
  • This indicates that Sulfolobus has a TCA cycle system similar to that found in mitochondria of eukaryotes. (wikipedia.org)
  • Sulfolobus is a genus of microorganism in the family Sulfolobaceae. (wikipedia.org)
  • The archaeon Sulfolobus solfataricus has a circular chromosome that consists of 2,992,245 bp. (wikipedia.org)
  • Among these, Sso Pox is a hyperthermostable enzyme isolated from the archaeon Sulfolobus solfataricus . (nature.com)
  • The elongation factor 1 alpha from the archaeon Sulfolobus solfataricus (SsEF-1 alpha) was expressed in Escherichia coli and purified. (uniparthenope.it)
  • Sulfolobus is now used as a model to study the molecular mechanisms of DNA replication in Archaea. (wikipedia.org)
  • Reference: Insertion of dNTPs opposite the 1,N2-propanodeoxyguanosine adduct by Sulfolobus solfataricus P2 DNA polymerase IV. (neb.com)
  • We conclude that differences in the Hoogsteen hydrogen bonding between nucleotides is the main factor in the preferential selectivity of dTTP opposite O(6)-methylG by human pol ι, in contrast to the mispairing modes observed previously for O(6)-methylG in the structures of the model DNA polymerases Sulfolobus solfataricus Dpo4 and Bacillus stearothermophilus DNA polymerase I. (nih.gov)
  • 7. Efficient and high fidelity incorporation of dCTP opposite 7,8-dihydro-8-oxodeoxyguanosine by Sulfolobus solfataricus DNA polymerase Dpo4. (nih.gov)
  • 20. Formation of purine-purine mispairs by Sulfolobus solfataricus DNA polymerase IV. (nih.gov)
  • Mapping of lysine methylation sites (indicated in yellow) on the crystal structure of the RNA polymerase from Sulfolobus shibatae, a hyperthermophilic, acidophilic crenarchaeon. (asmblog.org)
  • Using mass spectrometry, they identified 21 singly-methylated lysines across 9 subunits of the RNA polymerase isolated from Sulfolobus solfataricus . (asmblog.org)
  • The discovery of Sulfolobus , along with the previously isolated Thermus aquaticus (source of the extremely thermostable Taq DNA polymerase), is generally credited with launching the field of hyperthermophilic microbiology. (montana.edu)
  • The nonenveloped, rod-shaped virus SIRV2 (Sulfolobus islandicus rod-shaped virus 2) infects a microscopic organism known as Sulfolobus islandicus. (pasteur.fr)
  • The genome of the hyperthermophilic microorganism Sulfolobus islandicus (S. islandicus) harbors a unique leucyl-tRNA synthetase paralog, LeuRS-I, of unknown function. (illinoisstate.edu)
  • In addition, Sulfolobus islandicus isolates from different areas in Russia, Iceland, and the USA have been shown to be genetically distinct from each other making this organism useful for comparative analysis. (up.ac.za)
  • Sulfolobus is a genus of microorganism in the family Sulfolobaceae. (wikipedia.org)
  • The structure of the gamma subunit of archaeal translation initiation factor 2 (aIF2) from Sulfolobus solfataricus (SsoIF2gamma) was determined in complex with GDPCP (a GTP analog). (proteopedia.org)
  • Red coloration on rocks near Naples, Italy, produced by the hyperthermophile Sulfolobus solfataricus . (asmblog.org)
  • Since this step is important for an aerobic microorganism like Sulfolobus, it probably uses a different molecule for the same function or has a different pathway. (wikipedia.org)
  • Four enzymes of the gluconeogenic pathway in Sulfolobus solfataricus were purified and kinetically characterized. (sysmo-db.org)
  • We studied the fates of various components of the Sulfolobus solfataricus transcriptional apparatus under different stresses and found that in cells incubated at 90 degrees C for 1 h, transcription factor E (TFE) is selectively depleted, but its mRNA levels are increased. (aku.edu)
  • Sulfolobus was first discovered by Thomas Brock and colleagues in 1970 and formally described in 1972. (montana.edu)
  • Icelandic hot springs are home to the heat- and acid-loving virus SIRV2, which infects a microbe called Sulfolobus islandicus. (nih.gov)
  • It infects Sulfolobus islandicus, a microbe that lives in acidic Icelandic hot springs with temperatures topping 175 degrees Fahrenheit. (nih.gov)
  • Sulfolobus is an aerobic chemolithotroph that oxidizes H 2 S or S 0 to H 2 SO 4 and fixes CO 2 as sole carbon source. (montana.edu)
  • Besides the aerobic respiration of sulfur or organic compounds, Sulfolobus can also oxidize Fe 2+ to Fe 3+ , and this has been applied to the high-temperature leaching of iron and copper ores. (montana.edu)
  • The PARPSso thermoprotein from Sulfolobus solfataricus has been identified as a PARP-like enzyme that cleaves -NAD+ to synthesize oligomers of ADP-ribose and cross-reacts with polyclonal anti-PARP-1 catalytic site antibodies. (unina.it)
  • Sulfolobus cells are irregularly shaped and flagellar. (wikipedia.org)
  • Cells of Sulfolobus are more or less spherical but form distinct lobes. (montana.edu)
  • Sulfolobus can also grow chemoorganotrophically. (montana.edu)