A broad category of enzymes that are involved in the process of GENETIC RECOMBINATION.
Recombinases that insert exogenous DNA into the host genome. Examples include proteins encoded by the POL GENE of RETROVIRIDAE and also by temperate BACTERIOPHAGES, the best known being BACTERIOPHAGE LAMBDA.
Enzymes that catalyze the incorporation of deoxyribonucleotides into a chain of DNA. EC 2.7.7.-.
Production of new arrangements of DNA by various mechanisms such as assortment and segregation, CROSSING OVER; GENE CONVERSION; GENETIC TRANSFORMATION; GENETIC CONJUGATION; GENETIC TRANSDUCTION; or mixed infection of viruses.
Specific loci on both the bacterial DNA (attB) and the phage DNA (attP) which delineate the sites where recombination takes place between them, as the phage DNA becomes integrated (inserted) into the BACTERIAL DNA during LYSOGENY.
A family of recombinases initially identified in BACTERIA. They catalyze the ATP-driven exchange of DNA strands in GENETIC RECOMBINATION. The product of the reaction consists of a duplex and a displaced single-stranded loop, which has the shape of the letter D and is therefore called a D-loop structure.
A Rec A recombinase found in eukaryotes. Rad51 is involved in DNA REPAIR of double-strand breaks.
Recombinases that involved in the propagation of DNA TRANSPOSONS. They bind to transposon sequences found at two different sites along the same stretch of DNA and bring them into close proximity. The enzymes then catalyze the double strand cleavage, exchange of double strands and rejoining of DNA helices so that the DNA transposon is formed into a circular PLASMID.
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.
A temperate inducible phage and type species of the genus lambda-like viruses, in the family SIPHOVIRIDAE. Its natural host is E. coli K12. Its VIRION contains linear double-stranded DNA with single-stranded 12-base 5' sticky ends. The DNA circularizes on infection.
A cross-shaped DNA structure that can be observed under the electron microscope. It is formed by the incomplete exchange of strands between two double-stranded helices or by complementary INVERTED REPEAT SEQUENCES that refold into hairpin loops on opposite strands across from each other.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Permanganic acid (HMnO4), potassium salt. A highly oxidative, water-soluble compound with purple crystals, and a sweet taste. (From McGraw-Hill Dictionary of Scientific and Technical Information, 4th ed)
Proteins obtained from ESCHERICHIA COLI.
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.
Viruses whose hosts are bacterial cells.
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.
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.
Deoxyribonucleic acid that makes up the genetic material of bacteria.
A type of CELL NUCLEUS division, occurring during maturation of the GERM CELLS. Two successive cell nucleus divisions following a single chromosome duplication (S PHASE) result in daughter cells with half the number of CHROMOSOMES as the parent cells.
Enzymes that recombine DNA segments by a process which involves the formation of a synapse between two DNA helices, the cleavage of single strands from each DNA helix and the ligation of a DNA strand from one DNA helix to the other. The resulting DNA structure is called a Holliday junction which can be resolved by DNA REPLICATION or by HOLLIDAY JUNCTION RESOLVASES.
Structures within the nucleus of bacterial cells consisting of or containing DNA, which carry genetic information essential to the cell.
Discrete segments of DNA which can excise and reintegrate to another site in the genome. Most are inactive, i.e., have not been found to exist outside the integrated state. DNA transposable elements include bacterial IS (insertion sequence) elements, Tn elements, the maize controlling elements Ac and Ds, Drosophila P, gypsy, and pogo elements, the human Tigger elements and the Tc and mariner elements which are found throughout the animal kingdom.
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.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A reaction that severs one of the covalent sugar-phosphate linkages between NUCLEOTIDES that compose the sugar phosphate backbone of DNA. It is catalyzed enzymatically, chemically or by radiation. Cleavage may be exonucleolytic - removing the end nucleotide, or endonucleolytic - splitting the strand in two.
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).
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.
Directed modification of the gene complement of a living organism by such techniques as altering the DNA, substituting genetic material by means of a virus, transplanting whole nuclei, transplanting cell hybrids, etc.
Proteins found in any species of bacterium.
Insertion of viral DNA into host-cell DNA. This includes integration of phage DNA into bacterial DNA; (LYSOGENY); to form a PROPHAGE or integration of retroviral DNA into cellular DNA to form a PROVIRUS.
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 single chain of deoxyribonucleotides that occurs in some bacteria and viruses. It usually exists as a covalently closed circle.
Proteins found in any species of virus.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
An aberration in which a chromosomal segment is deleted and reinserted in the same place but turned 180 degrees from its original orientation, so that the gene sequence for the segment is reversed with respect to that of the rest of the chromosome.
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Circular duplex DNA isolated from viruses, bacteria and mitochondria in supercoiled or supertwisted form. This superhelical DNA is endowed with free energy. During transcription, the magnitude of RNA initiation is proportional to the DNA superhelicity.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.
Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes.
A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.
Theoretical representations that simulate the behavior or activity of genetic processes or phenomena. They include the use of mathematical equations, computers, and other electronic equipment.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The integration of exogenous DNA into the genome of an organism at sites where its expression can be suitably controlled. This integration occurs as a result of homologous recombination.
A parasexual process in BACTERIA; ALGAE; FUNGI; and ciliate EUKARYOTA for achieving exchange of chromosome material during fusion of two cells. In bacteria, this is a uni-directional transfer of genetic material; in protozoa it is a bi-directional exchange. In algae and fungi, it is a form of sexual reproduction, with the union of male and female gametes.
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.
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.
A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.
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.
Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.
Proteins that control the CELL DIVISION CYCLE. This family of proteins includes a wide variety of classes, including CYCLIN-DEPENDENT KINASES, mitogen-activated kinases, CYCLINS, and PHOSPHOPROTEIN PHOSPHATASES as well as their putative substrates such as chromatin-associated proteins, CYTOSKELETAL PROTEINS, and TRANSCRIPTION FACTORS.
The reconstruction of a continuous two-stranded DNA molecule without mismatch from a molecule which contained damaged regions. The major repair mechanisms are excision repair, in which defective regions in one strand are excised and resynthesized using the complementary base pairing information in the intact strand; photoreactivation repair, in which the lethal and mutagenic effects of ultraviolet light are eliminated; and post-replication repair, in which the primary lesions are not repaired, but the gaps in one daughter duplex are filled in by incorporation of portions of the other (undamaged) daughter duplex. Excision repair and post-replication repair are sometimes referred to as "dark repair" because they do not require light.
Mutagenesis where the mutation is caused by the introduction of foreign DNA sequences into a gene or extragenic sequence. This may occur spontaneously in vivo or be experimentally induced in vivo or in vitro. Proviral DNA insertions into or adjacent to a cellular proto-oncogene can interrupt GENETIC TRANSLATION of the coding sequences or interfere with recognition of regulatory elements and cause unregulated expression of the proto-oncogene resulting in tumor formation.
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.
Genes that are introduced into an organism using GENE TRANSFER TECHNIQUES.

Evolutionary relationships of pathogenic clones of Vibrio cholerae by sequence analysis of four housekeeping genes. (1/1464)

Studies of the Vibrio cholerae population, using molecular typing techniques, have shown the existence of several pathogenic clones, mainly sixth-pandemic, seventh-pandemic, and U.S. Gulf Coast clones. However, the relationship of the pathogenic clones to environmental V. cholerae isolates remains unclear. A previous study to determine the phylogeny of V. cholerae by sequencing the asd (aspartate semialdehyde dehydrogenase) gene of V. cholerae showed that the sixth-pandemic, seventh-pandemic, and U.S. Gulf Coast clones had very different asd sequences which fell into separate lineages in the V. cholerae population. As gene trees drawn from a single gene may not reflect the true topology of the population, we sequenced the mdh (malate dehydrogenase) and hlyA (hemolysin A) genes from representatives of environmental and clinical isolates of V. cholerae and found that the mdh and hlyA sequences from the three pathogenic clones were identical, except for the previously reported 11-bp deletion in hlyA in the sixth-pandemic clone. Identical sequences were obtained, despite average nucleotide differences in the mdh and hlyA genes of 1.52 and 3.25%, respectively, among all the isolates, suggesting that the three pathogenic clones are closely related. To extend these observations, segments of the recA and dnaE genes were sequenced from a selection of the pathogenic isolates, where the sequences were either identical or substantially different between the clones. The results show that the three pathogenic clones are very closely related and that there has been a high level of recombination in their evolution.  (+info)

Characterization of a Caenorhabditis elegans recA-like gene Ce-rdh-1 involved in meiotic recombination. (2/1464)

A recA-like gene was identified in the Caenorhabditis elegans genome project database. The putative product of the gene, termed Ce-rdh-1 (C. elegans RAD51 and DMC1/LIM15 homolog 1), consists of 357 amino acid residues. The predicted amino acid sequence of Ce-rdh-1 showed 46-60% identity to both RAD51 type and DMC1/LIM15 type genes in several eukaryote species. The results of RNAi (RNA-mediated interference) indicated that repression of Ce-rdh-1 blocked chromosome condensation of six bivalents and dissociation of chiasmata in oocytes of F1 progeny. Oogenesis did not proceed to the diakinesis stage. Accordingly, all the eggs produced (F2) died in early stages. These results suggest that Ce-rdh-1 participates in meiotic recombination.  (+info)

RecA-Mediated gene conversion and aminoglycoside resistance in strains heterozygous for rRNA. (3/1464)

Clinical resistance to aminoglycosides in general is due to enzymatic drug modification. Mutational alterations of the small ribosomal subunit rRNA have recently been found to mediate acquired resistance in bacterial pathogens in vivo. In this study we investigated the effect of 16S rRNA heterozygosity (wild-type [wt] and mutant [mut] operons at position 1408 [1408wt/1408mut]) on aminoglycoside resistance. Using an integrative vector, we introduced a single copy of a mutated rRNA operon (1408 A-->G) into Mycobacterium smegmatis, which carries two chromosomal wild-type rRNA operons; the resultant transformants exhibited an aminoglycoside-sensitive phenotype. In contrast, introduction of the mutated rRNA operon into an M. smegmatis rrnB knockout strain carrying a single functional chromosomal wild-type rRNA operon resulted in aminoglycoside-resistant transformants. Subsequent analysis by DNA sequencing and RNase protection assays unexpectedly demonstrated a homozygous mutant genotype, rRNAmut/rRNAmut, in the resistant transformants. To investigate whether RecA-mediated gene conversion was responsible for the aminoglycoside-resistant phenotype in the rRNAwt/rRNAmut strains, recA mutant strains were generated by allelic exchange techniques. Transformation of the recA rrnB M. smegmatis mutant strains with an integrative vector expressing a mutated rRNA operon (Escherichia coli position 1408 A-->G) resulted in transformants with an aminoglycoside-sensitive phenotype. Subsequent analysis showed stable heterozygosity at 16S rRNA position 1408 with a single wild-type allele and a single resistant allele. These results demonstrate that rRNA-mediated mutational resistance to aminoglycosides is recessive.  (+info)

A unique DNase activity shares the active site with ATPase activity of the RecA/Rad51 homologue (Pk-REC) from a hyperthermophilic archaeon. (4/1464)

A RecA/Rad51 homologue from Pyrococcus kodakaraensis KOD1 (Pk-REC) is the smallest protein among various RecA/Rad51 homologues. Nevertheless, Pk-Rec is a super multifunctional protein and shows a deoxyribonuclease activity. This deoxyribonuclease activity was inhibited by 3 mM or more ATP, suggesting that the catalytic centers of the ATPase and deoxyribonuclease activities are overlapped. To examine whether these two enzymatic activities share the same active site, a number of site-directed mutations were introduced into Pk-REC and the ATPase and deoxyribonuclease activities of the mutant proteins were determined. The mutant enzyme in which double mutations Lys-33 to Ala and Thr-34 to Ala were introduced, fully lost both of these activities, indicating that Lys-33 and/or Thr-34 are important for both ATPase and deoxyribonuclease activities. The mutation of Asp-112 to Ala slightly and almost equally reduced both ATPase and deoxyribonuclease activities. In addition, the mutation of Glu-54 to Gln did not seriously affect the ATPase, deoxyribonuclease, and UV tolerant activities. These results strongly suggest that the active sites of the ATPase and deoxyribonuclease activities of Pk-REC are common. It is noted that unlike Glu-96 in Escherichia coli RecA, which has been proposed to be a catalytic residue for the ATPase activity, the corresponding residual Glu-54 in Pk-REC is not involved in the catalytic function of the protein.  (+info)

Rapid and sensitive quantification of Borrelia burgdorferi-infected mouse tissues by continuous fluorescent monitoring of PCR. (5/1464)

The quantity of Borrelia burgdorferi organisms in tissue samples is an important determinant for infection studies in the mouse model of Lyme disease. This report presents the development of a rapid and sensitive external-standard-based PCR assay for the absolute quantification of B. burgdorferi in mouse tissue samples. The assay uses a double-stranded DNA dye to continuously monitor product formation and in less than an hour was able to quantify samples ranging up to 6 log units in concentration. The PCR efficiencies of the sample and the standard were matched by using a standard composed of purified B. burgdorferi chromosome mixed with tissue-matched mouse genome lacking bacterial DNA. Normalization of B. burgdorferi quantities to the mouse nidogen gene allowed comparison of B. burgdorferi numbers in samples isolated from different tissues and strains. PCR analysis of the chromosomal gene recA in cultured B. burgdorferi was consistent with a single recA per bacterium. The parameters defined in this assay should be applicable to quantification of other organisms, even infectious agents for which no ready source of DNA standard is available. In summary, this report presents a rapid external-standard-based PCR method for the quantification of B. burgdorferi in mouse DNA samples.  (+info)

The Mycobacterium tuberculosis recA intein can be used in an ORFTRAP to select for open reading frames. (6/1464)

The DNA repair protein RecA of Mycobacterium tuberculosis contains an intein, a self-splicing protein element. We have employed this Mtu recA intein to create a selection system for successful intein splicing by inserting it into a kanamycin-resistance gene so that functional antibiotic resistance can only be restored upon protein splicing. We then proceeded to develop an ORFTRAP, i.e., a selection system for the cloning of open reading frames (ORFs). The ORFTRAP exploits the self-splicing properties of inteins (which depend on full-length in-frame translation of a precursor protein) by allowing protein splicing to occur when DNA fragments encoding ORFs are inserted into the Mtu recA intein, whereas DNA fragments containing non-ORFs are selected against. Regions of the Mtu recA intein that tolerate the insertion of additional amino acids were identified by Bgl II linker scanning mutagenesis, and a respective construct was chosen as the ORFTRAP. To test the maximum insert size that could be cloned into ORFTRAP, DNA fragments of increasing length from the Listeria monocytogenes hly gene as well as a genomic library of Haemophilus influenzae were inserted and it was found that the longest permissive inserts were 425 bp and 251 bp, respectively. The H. influenzae ORFTRAP library also demonstrated the strength (strong selection power) and weakness (insertion of very small fragments) of the system. Further modifications should make the ORFTRAP useful for protein expression, epitope mapping, and antigen screening.  (+info)

Characterization of thermostable RecA protein and analysis of its interaction with single-stranded DNA. (7/1464)

Thermostable RecA protein (ttRecA) from Thermus thermophilus HB8 showed strand exchange activity at 65 degrees C but not at 37 degrees C, although nucleoprotein complex was observed at both temperatures. ttRecA showed single-stranded DNA (ssDNA)-dependent ATPase activity, and its activity was maximal at 65 degrees C. The kinetic parameters, K(m) and kcat, for adenosine triphosphate (ATP) hydrolysis with poly(dT) were 1.4 mM and 0.60 s-1 at 65 degrees C, and 0.34 mM and 0.28 s-1 at 37 degrees C, respectively. Substrate cooperativity was observed at both temperatures, and the Hill coefficient was about 2. At 65 degrees C, all tested ssDNAs were able to stimulate the ATPase activity. The order of ATPase stimulation was: poly(dC) > poly(dT) > M13 ssDNA > poly(dA). Double-stranded DNAs (dsDNA), poly(dT).poly(dA) and M13 dsDNA, were unable to activate the enzyme at 65 degrees C. At 37 degrees C, however, not only dsDNAs but also poly(dA) and M13 ssDNA showed poor stimulating ability. At 25 degrees C, poly(dA) and M13 ssDNA gave circular dichroism (CD) peaks at around 192 nm, which reflect a particular structure of DNA. The conformation was changed by an upshift of temperature or binding to Escherichia coli RecA protein (ecRecA), but not to ttRecA. The dissociation constant between ecRecA and poly(dA) was estimated to be 44 microM at 25 degrees C by the change in the CD. These observations suggest that the capability to modify the conformation of ssDNA may be different between ttRecA and ecRecA. The specific structure of ssDNA was altered by heat or binding of ecRecA. After this alteration, ttRecA and ecRecA can express their activities at each physiological temperature.  (+info)

Induction of prophages of enterohemorrhagic Escherichia coli O157:H7 with norfloxacin. (8/1464)

Norfloxacin (NFLX) caused induction of prophages VT1 and VT2 of enterohemorrhagic Escherichia coli O157 at subinhibitory concentrations. In time course experiments, we observed the following sequential events: upon induction, the phage genomes underwent multiplication; the amount of stx genes increased; and subsequently, large quantities of toxins VT1 and VT2 were produced. Further studies showed that the molecular mechanism of prophage induction is closely related to the RecA system since the prophage VT2 was not induced with NFLX in a recA mutant strain.  (+info)

Recombinases are enzymes that catalyze the process of recombination between two or more DNA molecules by breaking and rejoining their strands. They play a crucial role in various biological processes such as DNA repair, genetic recombination during meiosis, and site-specific genetic modifications.

Recombinases recognize and bind to specific DNA sequences, called recognition sites or crossover sites, where they cleave the phosphodiester bonds of the DNA backbone, forming a Holliday junction intermediate. The recombinase then catalyzes the exchange of strands between the two DNA molecules at the junction and subsequently ligates the broken ends to form new phosphodiester bonds, resulting in the recombination of the DNA molecules.

There are several types of recombinases, including serine recombinases, tyrosine recombinases, and lambda integrase. These enzymes differ in their recognition sites, catalytic mechanisms, and biological functions. Recombinases have important applications in molecular biology and genetic engineering, such as generating targeted DNA deletions or insertions, constructing genetic circuits, and developing gene therapy strategies.

Integrases are enzymes that are responsible for the integration of genetic material into a host's DNA. In particular, integrases play a crucial role in the life cycle of retroviruses, such as HIV (Human Immunodeficiency Virus). These viruses have an RNA genome, which must be reverse-transcribed into DNA before it can be integrated into the host's chromosomal DNA.

The integrase enzyme, encoded by the virus's pol gene, is responsible for this critical step in the retroviral replication cycle. It mediates the cutting and pasting of the viral cDNA into a specific site within the host cell's genome, leading to the formation of a provirus. This provirus can then be transcribed and translated by the host cell's machinery, resulting in the production of new virus particles.

Integrase inhibitors are an important class of antiretroviral drugs used in the treatment of HIV infection. They work by blocking the activity of the integrase enzyme, thereby preventing the integration of viral DNA into the host genome and halting the replication of the virus.

DNA nucleotidyltransferases are a class of enzymes that catalyze the addition of one or more nucleotides to the 3'-hydroxyl end of a DNA molecule. These enzymes play important roles in various biological processes, including DNA repair, recombination, and replication.

The reaction catalyzed by DNA nucleotidyltransferases involves the transfer of a nucleotide triphosphate (NTP) to the 3'-hydroxyl end of a DNA molecule, resulting in the formation of a phosphodiester bond and the release of pyrophosphate. The enzymes can add a single nucleotide or multiple nucleotides, depending on the specific enzyme and its function.

DNA nucleotidyltransferases are classified into several subfamilies based on their sequence similarity and function, including polymerases, terminal transferases, and primases. These enzymes have been extensively studied for their potential applications in biotechnology and medicine, such as in DNA sequencing, diagnostics, and gene therapy.

Genetic recombination is the process by which genetic material is exchanged between two similar or identical molecules of DNA during meiosis, resulting in new combinations of genes on each chromosome. This exchange occurs during crossover, where segments of DNA are swapped between non-sister homologous chromatids, creating genetic diversity among the offspring. It is a crucial mechanism for generating genetic variability and facilitating evolutionary change within populations. Additionally, recombination also plays an essential role in DNA repair processes through mechanisms such as homologous recombinational repair (HRR) and non-homologous end joining (NHEJ).

Attachment sites in microbiology refer to specific locations on the surface of a host cell (such as a human or animal cell) where microorganisms such as bacteria, viruses, fungi, or parasites can bind and establish an infection. These sites may be receptors, proteins, or other molecules on the cell surface that the microorganism recognizes and interacts with through its own adhesive structures, such as pili or fimbriae in bacteria, or glycoprotein spikes in viruses. The ability of a microorganism to attach to a host cell is a critical first step in the infection process, and understanding these attachment sites can provide important insights into the pathogenesis of infectious diseases and potential targets for prevention and treatment.

Recombination is a natural process that occurs in cells to exchange genetic information between two similar or identical strands of DNA. This process helps to maintain the stability and diversity of the genome. RecA (RecA protein) is a type of recombinase enzyme found in bacteria, including Escherichia coli, that plays a crucial role in this process.

RecA recombinases are proteins that facilitate the exchange of genetic information between two DNA molecules by promoting homologous pairing and strand exchange. Homologous pairing is the alignment of similar or identical sequences of nucleotides on two different DNA molecules, while strand exchange refers to the physical transfer of one strand of DNA from one molecule to another.

RecA recombinases work by forming a nucleoprotein filament on single-stranded DNA (ssDNA) and then searching for complementary sequences on double-stranded DNA (dsDNA). Once a complementary sequence is found, the RecA protein facilitates the invasion of the ssDNA into the dsDNA, leading to strand exchange and the formation of a joint molecule. This joint molecule can then be used as a template for DNA replication or repair.

RecA recombinases have been extensively studied due to their importance in genetic recombination and DNA repair. They also have potential applications in biotechnology, such as in the development of genome engineering tools and methods for detecting and quantifying specific DNA sequences.

Rad51 recombinase is a protein involved in the repair of double-stranded DNA breaks through homologous recombination, a process that helps maintain genomic stability. This protein forms a nucleoprotein filament on single-stranded DNA, facilitating the search for and invasion of homologous sequences in double-stranded DNA. Rad51 recombinase is highly conserved across various species, including humans, and plays a crucial role in preventing genetic disorders, cancer, and aging caused by DNA damage.

Transposon resolvases are enzymes that catalyze the precise excision of transposable elements, also known as transposons or jumping genes, from DNA molecules. Transposons are mobile genetic elements that can move and integrate into different locations within a genome. This movement can lead to genetic variation, but it can also cause mutations, genomic instability, and other deleterious effects.

Transposon resolvases function by cleaving specific sites within the transposable element, resulting in the formation of a circular DNA molecule called a transposon circle. The transposon circle can then be reintegrated into the genome at a new location, or it can be degraded by cellular enzymes.

Transposon resolvases are essential for the proper regulation and mobility of transposable elements in many organisms, including bacteria, yeast, and plants. Defects in transposon resolvase function can lead to genomic instability, developmental abnormalities, and other phenotypic consequences.

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.

Bacteriophage lambda, often simply referred to as phage lambda, is a type of virus that infects the bacterium Escherichia coli (E. coli). It is a double-stranded DNA virus that integrates its genetic material into the bacterial chromosome as a prophage when it infects the host cell. This allows the phage to replicate along with the bacterium until certain conditions trigger the lytic cycle, during which new virions are produced and released by lysing, or breaking open, the host cell.

Phage lambda is widely studied in molecular biology due to its well-characterized life cycle and genetic structure. It has been instrumental in understanding various fundamental biological processes such as gene regulation, DNA recombination, and lysis-lysogeny decision.

"Cruciform DNA" is a term used to describe a specific conformation or structure that a double-stranded DNA molecule can adopt. It is so-called because the structure resembles the shape of a cross or crucifix.

This conformation arises when two inverted repeats of DNA sequence are located close to each other on the same DNA molecule, such that they can pair up and form a stable secondary structure. This results in the formation of a hairpin loop at each end of the inverted repeat sequences, with the loops pointing towards each other and the intervening sequences forming two arms that cross in the middle.

Cruciform structures are important in various biological processes, including DNA replication, repair, and recombination. However, they can also pose challenges to these processes, as the crossing of the DNA strands can create topological constraints that must be resolved before replication or transcription can proceed.

It's worth noting that cruciform structures are not stable in solution and are usually only observed under specific conditions, such as when the DNA is supercoiled or when negative supercoiling is introduced through the action of enzymes like topoisomerases.

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.

Potassium permanganate is not a medical term, but it is a chemical compound with the formula KMnO4. It's a dark purple crystalline solid that is soluble in water and has strong oxidizing properties. In a medical context, potassium permanganate is occasionally used as a topical antiseptic and disinfectant, particularly for treating minor wounds, burns, and ulcers. It's also used to treat certain skin conditions such as eczema and psoriasis. However, its use is limited due to the potential for skin irritation and staining of the skin and clothing. It should always be used under medical supervision and with caution.

'Escherichia coli (E. coli) proteins' refer to the various types of proteins that are produced and expressed by the bacterium Escherichia coli. These proteins play a critical role in the growth, development, and survival of the organism. They are involved in various cellular processes such as metabolism, DNA replication, transcription, translation, repair, and regulation.

E. coli is a gram-negative, facultative anaerobe that is commonly found in the intestines of warm-blooded organisms. It is widely used as a model organism in scientific research due to its well-studied genetics, rapid growth, and ability to be easily manipulated in the laboratory. As a result, many E. coli proteins have been identified, characterized, and studied in great detail.

Some examples of E. coli proteins include enzymes involved in carbohydrate metabolism such as lactase, sucrase, and maltose; proteins involved in DNA replication such as the polymerases, single-stranded binding proteins, and helicases; proteins involved in transcription such as RNA polymerase and sigma factors; proteins involved in translation such as ribosomal proteins, tRNAs, and aminoacyl-tRNA synthetases; and regulatory proteins such as global regulators, two-component systems, and transcription factors.

Understanding the structure, function, and regulation of E. coli proteins is essential for understanding the basic biology of this important organism, as well as for developing new strategies for combating bacterial infections and improving industrial processes involving bacteria.

'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.

Bacteriophages, often simply called phages, are viruses that infect and replicate within bacteria. They consist of a protein coat, called the capsid, that encases the genetic material, which can be either DNA or RNA. Bacteriophages are highly specific, meaning they only infect certain types of bacteria, and they reproduce by hijacking the bacterial cell's machinery to produce more viruses.

Once a phage infects a bacterium, it can either replicate its genetic material and create new phages (lytic cycle), or integrate its genetic material into the bacterial chromosome and replicate along with the bacterium (lysogenic cycle). In the lytic cycle, the newly formed phages are released by lysing, or breaking open, the bacterial cell.

Bacteriophages play a crucial role in shaping microbial communities and have been studied as potential alternatives to antibiotics for treating bacterial infections.

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.

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.

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.

Meiosis is a type of cell division that results in the formation of four daughter cells, each with half the number of chromosomes as the parent cell. It is a key process in sexual reproduction, where it generates gametes or sex cells (sperm and eggs).

The process of meiosis involves one round of DNA replication followed by two successive nuclear divisions, meiosis I and meiosis II. In meiosis I, homologous chromosomes pair, form chiasma and exchange genetic material through crossing over, then separate from each other. In meiosis II, sister chromatids separate, leading to the formation of four haploid cells. This process ensures genetic diversity in offspring by shuffling and recombining genetic information during the formation of gametes.

Transposases are a type of enzyme that are involved in the process of transposition, which is the movement of a segment of DNA from one location within a genome to another. Transposases recognize and bind to specific sequences of DNA called inverted repeats that flank the mobile genetic element, or transposon, and catalyze the excision and integration of the transposon into a new location in the genome. This process can have significant consequences for the organization and regulation of genes within an organism's genome, and may contribute to genetic diversity and evolution.

Bacterial chromosomes are typically circular, double-stranded DNA molecules that contain the genetic material of bacteria. Unlike eukaryotic cells, which have their DNA housed within a nucleus, bacterial chromosomes are located in the cytoplasm of the cell, often associated with the bacterial nucleoid.

Bacterial chromosomes can vary in size and structure among different species, but they typically contain all of the genetic information necessary for the survival and reproduction of the organism. They may also contain plasmids, which are smaller circular DNA molecules that can carry additional genes and can be transferred between bacteria through a process called conjugation.

One important feature of bacterial chromosomes is their ability to replicate rapidly, allowing bacteria to divide quickly and reproduce in large numbers. The replication of the bacterial chromosome begins at a specific origin point and proceeds in opposite directions until the entire chromosome has been copied. This process is tightly regulated and coordinated with cell division to ensure that each daughter cell receives a complete copy of the genetic material.

Overall, the study of bacterial chromosomes is an important area of research in microbiology, as understanding their structure and function can provide insights into bacterial genetics, evolution, and pathogenesis.

DNA transposable elements, also known as transposons or jumping genes, are mobile genetic elements that can change their position within a genome. They are composed of DNA sequences that include genes encoding the enzymes required for their own movement (transposase) and regulatory elements. When activated, the transposase recognizes specific sequences at the ends of the element and catalyzes the excision and reintegration of the transposable element into a new location in the genome. This process can lead to genetic variation, as the insertion of a transposable element can disrupt the function of nearby genes or create new combinations of gene regulatory elements. Transposable elements are widespread in both prokaryotic and eukaryotic genomes and are thought to play a significant role in genome evolution.

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.

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 cleavage is the breaking of the phosphodiester bonds in the DNA molecule, resulting in the separation of the two strands of the double helix. This process can occur through chemical or enzymatic reactions and can result in various types of damage to the DNA molecule, including single-strand breaks, double-strand breaks, and base modifications.

Enzymatic DNA cleavage is typically carried out by endonucleases, which are enzymes that cut DNA molecules at specific sequences or structures. There are two main types of endonucleases: restriction endonucleases and repair endonucleases. Restriction endonucleases recognize and cleave specific DNA sequences, often used in molecular biology techniques such as genetic engineering and cloning. Repair endonucleases, on the other hand, are involved in DNA repair processes and recognize and cleave damaged or abnormal DNA structures.

Chemical DNA cleavage can occur through various mechanisms, including oxidation, alkylation, or hydrolysis of the phosphodiester bonds. Chemical agents such as hydrogen peroxide, formaldehyde, or hydrazine can induce chemical DNA cleavage and are often used in laboratory settings for various purposes, such as DNA fragmentation or labeling.

Overall, DNA cleavage is an essential process in many biological functions, including DNA replication, repair, and recombination. However, excessive or improper DNA cleavage can lead to genomic instability, mutations, and cell death.

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.

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.

Genetic engineering, also known as genetic modification, is a scientific process where the DNA or genetic material of an organism is manipulated to bring about a change in its characteristics. This is typically done by inserting specific genes into the organism's genome using various molecular biology techniques. These new genes may come from the same species (cisgenesis) or a different species (transgenesis). The goal is to produce a desired trait, such as resistance to pests, improved nutritional content, or increased productivity. It's widely used in research, medicine, and agriculture. However, it's important to note that the use of genetically engineered organisms can raise ethical, environmental, and health concerns.

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.

Virus integration, in the context of molecular biology and virology, refers to the insertion of viral genetic material into the host cell's genome. This process is most commonly associated with retroviruses, such as HIV (Human Immunodeficiency Virus), which have an enzyme called reverse transcriptase that converts their RNA genome into DNA. This DNA can then integrate into the host's chromosomal DNA, becoming a permanent part of the host's genetic material.

This integration is a crucial step in the retroviral life cycle, allowing the virus to persist within the host cell and evade detection by the immune system. It also means that the viral genome can be passed on to daughter cells when the host cell divides.

However, it's important to note that not all viruses integrate their genetic material into the host's genome. Some viruses, like influenza, exist as separate entities within the host cell and do not become part of the host's DNA.

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.

Single-stranded DNA (ssDNA) is a form of DNA that consists of a single polynucleotide chain. In contrast, double-stranded DNA (dsDNA) consists of two complementary polynucleotide chains that are held together by hydrogen bonds.

In the double-helix structure of dsDNA, each nucleotide base on one strand pairs with a specific base on the other strand through hydrogen bonding: adenine (A) with thymine (T), and guanine (G) with cytosine (C). This base pairing provides stability to the double-stranded structure.

Single-stranded DNA, on the other hand, lacks this complementary base pairing and is therefore less stable than dsDNA. However, ssDNA can still form secondary structures through intrastrand base pairing, such as hairpin loops or cruciform structures.

Single-stranded DNA is found in various biological contexts, including viral genomes, transcription bubbles during gene expression, and in certain types of genetic recombination. It also plays a critical role in some laboratory techniques, such as polymerase chain reaction (PCR) and DNA sequencing.

Viral proteins are the proteins that are encoded by the viral genome and are essential for the viral life cycle. These proteins can be structural or non-structural and play various roles in the virus's replication, infection, and assembly process. Structural proteins make up the physical structure of the virus, including the capsid (the protein shell that surrounds the viral genome) and any envelope proteins (that may be present on enveloped viruses). Non-structural proteins are involved in the replication of the viral genome and modulation of the host cell environment to favor viral replication. Overall, a thorough understanding of viral proteins is crucial for developing antiviral therapies and vaccines.

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.

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.

A chromosome inversion is a genetic rearrangement where a segment of a chromosome has been reversed end to end, so that its order of genes is opposite to the original. This means that the gene sequence on the segment of the chromosome has been inverted.

In an inversion, the chromosome breaks in two places, and the segment between the breaks rotates 180 degrees before reattaching. This results in a portion of the chromosome being inverted, or turned upside down, relative to the rest of the chromosome.

Chromosome inversions can be either paracentric or pericentric. Paracentric inversions involve a segment that does not include the centromere (the central constriction point of the chromosome), while pericentric inversions involve a segment that includes the centromere.

Inversions can have various effects on an individual's phenotype, depending on whether the inversion involves genes and if so, how those genes are affected by the inversion. In some cases, inversions may have no noticeable effect, while in others they may cause genetic disorders or predispose an individual to certain health conditions.

Tyrosine is an non-essential amino acid, which means that it can be synthesized by the human body from another amino acid called phenylalanine. Its name is derived from the Greek word "tyros," which means cheese, as it was first isolated from casein, a protein found in cheese.

Tyrosine plays a crucial role in the production of several important substances in the body, including neurotransmitters such as dopamine, norepinephrine, and epinephrine, which are involved in various physiological processes, including mood regulation, stress response, and cognitive functions. It also serves as a precursor to melanin, the pigment responsible for skin, hair, and eye color.

In addition, tyrosine is involved in the structure of proteins and is essential for normal growth and development. Some individuals may require tyrosine supplementation if they have a genetic disorder that affects tyrosine metabolism or if they are phenylketonurics (PKU), who cannot metabolize phenylalanine, which can lead to elevated tyrosine levels in the blood. However, it is important to consult with a healthcare professional before starting any supplementation regimen.

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.

Superhelical DNA refers to a type of DNA structure that is formed when the double helix is twisted around itself. This occurs due to the presence of negative supercoiling, which results in an overtwisted state that can be described as having a greater number of helical turns than a relaxed circular DNA molecule.

Superhelical DNA is often found in bacterial and viral genomes, where it plays important roles in compacting the genome into a smaller volume and facilitating processes such as replication and transcription. The degree of supercoiling can affect the structure and function of DNA, with varying levels of supercoiling influencing the accessibility of specific regions of the genome to proteins and other regulatory factors.

Superhelical DNA is typically maintained in a stable state by topoisomerase enzymes, which introduce or remove twists in the double helix to regulate its supercoiling level. Changes in supercoiling can have significant consequences for cellular processes, as they can impact the expression of genes and the regulation of chromosome structure and function.

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.

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.

Protein engineering is a branch of molecular biology that involves the modification of proteins to achieve desired changes in their structure and function. This can be accomplished through various techniques, including site-directed mutagenesis, gene shuffling, directed evolution, and rational design. The goal of protein engineering may be to improve the stability, activity, specificity, or other properties of a protein for therapeutic, diagnostic, industrial, or research purposes. It is an interdisciplinary field that combines knowledge from genetics, biochemistry, structural biology, and computational modeling.

A genetic complementation test is a laboratory procedure used in molecular genetics to determine whether two mutated genes can complement each other's function, indicating that they are located at different loci and represent separate alleles. This test involves introducing a normal or wild-type copy of one gene into a cell containing a mutant version of the same gene, and then observing whether the presence of the normal gene restores the normal function of the mutated gene. If the introduction of the normal gene results in the restoration of the normal phenotype, it suggests that the two genes are located at different loci and can complement each other's function. However, if the introduction of the normal gene does not restore the normal phenotype, it suggests that the two genes are located at the same locus and represent different alleles of the same gene. This test is commonly used to map genes and identify genetic interactions in a variety of organisms, including bacteria, yeast, and animals.

Genetic models are theoretical frameworks used in genetics to describe and explain the inheritance patterns and genetic architecture of traits, diseases, or phenomena. These models are based on mathematical equations and statistical methods that incorporate information about gene frequencies, modes of inheritance, and the effects of environmental factors. They can be used to predict the probability of certain genetic outcomes, to understand the genetic basis of complex traits, and to inform medical management and treatment decisions.

There are several types of genetic models, including:

1. Mendelian models: These models describe the inheritance patterns of simple genetic traits that follow Mendel's laws of segregation and independent assortment. Examples include autosomal dominant, autosomal recessive, and X-linked inheritance.
2. Complex trait models: These models describe the inheritance patterns of complex traits that are influenced by multiple genes and environmental factors. Examples include heart disease, diabetes, and cancer.
3. Population genetics models: These models describe the distribution and frequency of genetic variants within populations over time. They can be used to study evolutionary processes, such as natural selection and genetic drift.
4. Quantitative genetics models: These models describe the relationship between genetic variation and phenotypic variation in continuous traits, such as height or IQ. They can be used to estimate heritability and to identify quantitative trait loci (QTLs) that contribute to trait variation.
5. Statistical genetics models: These models use statistical methods to analyze genetic data and infer the presence of genetic associations or linkage. They can be used to identify genetic risk factors for diseases or traits.

Overall, genetic models are essential tools in genetics research and medical genetics, as they allow researchers to make predictions about genetic outcomes, test hypotheses about the genetic basis of traits and diseases, and develop strategies for prevention, diagnosis, and treatment.

Site-directed mutagenesis is a molecular biology technique used to introduce specific and targeted changes to a specific DNA sequence. This process involves creating a new variant of a gene or a specific region of interest within a DNA molecule by introducing a planned, deliberate change, or mutation, at a predetermined site within the DNA sequence.

The methodology typically involves the use of molecular tools such as PCR (polymerase chain reaction), restriction enzymes, and/or ligases to introduce the desired mutation(s) into a plasmid or other vector containing the target DNA sequence. The resulting modified DNA molecule can then be used to transform host cells, allowing for the production of large quantities of the mutated gene or protein for further study.

Site-directed mutagenesis is a valuable tool in basic research, drug discovery, and biotechnology applications where specific changes to a DNA sequence are required to understand gene function, investigate protein structure/function relationships, or engineer novel biological properties into existing genes or proteins.

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.

Gene targeting is a research technique in molecular biology used to precisely modify specific genes within the genome of an organism. This technique allows scientists to study gene function by creating targeted genetic changes, such as insertions, deletions, or mutations, in a specific gene of interest. The process typically involves the use of engineered nucleases, such as CRISPR-Cas9 or TALENs, to introduce double-stranded breaks at desired locations within the genome. These breaks are then repaired by the cell's own DNA repair machinery, often leading to the incorporation of designed changes in the targeted gene. Gene targeting is a powerful tool for understanding gene function and has wide-ranging applications in basic research, agriculture, and therapeutic development.

Genetic conjugation is a type of genetic transfer that occurs between bacterial cells. It involves the process of one bacterium (the donor) transferring a piece of its DNA to another bacterium (the recipient) through direct contact or via a bridge-like connection called a pilus. This transferred DNA may contain genes that provide the recipient cell with new traits, such as antibiotic resistance or virulence factors, which can make the bacteria more harmful or difficult to treat. Genetic conjugation is an important mechanism for the spread of antibiotic resistance and other traits among bacterial populations.

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.

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.

A conserved sequence in the context of molecular biology refers to a pattern of nucleotides (in DNA or RNA) or amino acids (in proteins) that has remained relatively unchanged over evolutionary time. These sequences are often functionally important and are highly conserved across different species, indicating strong selection pressure against changes in these regions.

In the case of protein-coding genes, the corresponding amino acid sequence is deduced from the DNA sequence through the genetic code. Conserved sequences in proteins may indicate structurally or functionally important regions, such as active sites or binding sites, that are critical for the protein's activity. Similarly, conserved non-coding sequences in DNA may represent regulatory elements that control gene expression.

Identifying conserved sequences can be useful for inferring evolutionary relationships between species and for predicting the function of unknown genes or proteins.

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.

Mutagenesis is the process by which the genetic material (DNA or RNA) of an organism is changed in a way that can alter its phenotype, or observable traits. These changes, known as mutations, can be caused by various factors such as chemicals, radiation, or viruses. Some mutations may have no effect on the organism, while others can cause harm, including diseases and cancer. Mutagenesis is a crucial area of study in genetics and molecular biology, with implications for understanding evolution, genetic disorders, and the development of new medical treatments.

Cell cycle proteins are a group of regulatory proteins that control the progression of the cell cycle, which is the series of events that take place in a eukaryotic cell leading to its division and duplication. These proteins can be classified into several categories based on their functions during different stages of the cell cycle.

The major groups of cell cycle proteins include:

1. Cyclin-dependent kinases (CDKs): CDKs are serine/threonine protein kinases that regulate key transitions in the cell cycle. They require binding to a regulatory subunit called cyclin to become active. Different CDK-cyclin complexes are activated at different stages of the cell cycle.
2. Cyclins: Cyclins are a family of regulatory proteins that bind and activate CDKs. Their levels fluctuate throughout the cell cycle, with specific cyclins expressed during particular phases. For example, cyclin D is important for the G1 to S phase transition, while cyclin B is required for the G2 to M phase transition.
3. CDK inhibitors (CKIs): CKIs are regulatory proteins that bind to and inhibit CDKs, thereby preventing their activation. CKIs can be divided into two main families: the INK4 family and the Cip/Kip family. INK4 family members specifically inhibit CDK4 and CDK6, while Cip/Kip family members inhibit a broader range of CDKs.
4. Anaphase-promoting complex/cyclosome (APC/C): APC/C is an E3 ubiquitin ligase that targets specific proteins for degradation by the 26S proteasome. During the cell cycle, APC/C regulates the metaphase to anaphase transition and the exit from mitosis by targeting securin and cyclin B for degradation.
5. Other regulatory proteins: Several other proteins play crucial roles in regulating the cell cycle, such as p53, a transcription factor that responds to DNA damage and arrests the cell cycle, and the polo-like kinases (PLKs), which are involved in various aspects of mitosis.

Overall, cell cycle proteins work together to ensure the proper progression of the cell cycle, maintain genomic stability, and prevent uncontrolled cell growth, which can lead to cancer.

DNA repair is the process by which cells identify and correct damage to the DNA molecules that encode their genome. DNA can be damaged by a variety of internal and external factors, such as radiation, chemicals, and metabolic byproducts. If left unrepaired, this damage can lead to mutations, which may in turn lead to cancer and other diseases.

There are several different mechanisms for repairing DNA damage, including:

1. Base excision repair (BER): This process repairs damage to a single base in the DNA molecule. An enzyme called a glycosylase removes the damaged base, leaving a gap that is then filled in by other enzymes.
2. Nucleotide excision repair (NER): This process repairs more severe damage, such as bulky adducts or crosslinks between the two strands of the DNA molecule. An enzyme cuts out a section of the damaged DNA, and the gap is then filled in by other enzymes.
3. Mismatch repair (MMR): This process repairs errors that occur during DNA replication, such as mismatched bases or small insertions or deletions. Specialized enzymes recognize the error and remove a section of the newly synthesized strand, which is then replaced by new nucleotides.
4. Double-strand break repair (DSBR): This process repairs breaks in both strands of the DNA molecule. There are two main pathways for DSBR: non-homologous end joining (NHEJ) and homologous recombination (HR). NHEJ directly rejoins the broken ends, while HR uses a template from a sister chromatid to repair the break.

Overall, DNA repair is a crucial process that helps maintain genome stability and prevent the development of diseases caused by genetic mutations.

Insertional mutagenesis is a process of introducing new genetic material into an organism's genome at a specific location, which can result in a change or disruption of the function of the gene at that site. This technique is often used in molecular biology research to study gene function and regulation. The introduction of the foreign DNA is typically accomplished through the use of mobile genetic elements, such as transposons or viruses, which are capable of inserting themselves into the genome.

The insertion of the new genetic material can lead to a loss or gain of function in the affected gene, resulting in a mutation. This type of mutagenesis is called "insertional" because the mutation is caused by the insertion of foreign DNA into the genome. The effects of insertional mutagenesis can range from subtle changes in gene expression to the complete inactivation of a gene.

This technique has been widely used in genetic research, including the study of developmental biology, cancer, and genetic diseases. It is also used in the development of genetically modified organisms (GMOs) for agricultural and industrial applications.

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.

A transgene is a segment of DNA that has been artificially transferred from one organism to another, typically between different species, to introduce a new trait or characteristic. The term "transgene" specifically refers to the genetic material that has been transferred and has become integrated into the host organism's genome. This technology is often used in genetic engineering and biomedical research, including the development of genetically modified organisms (GMOs) for agricultural purposes or the creation of animal models for studying human diseases.

Transgenes can be created using various techniques, such as molecular cloning, where a desired gene is isolated, manipulated, and then inserted into a vector (a small DNA molecule, such as a plasmid) that can efficiently enter the host organism's cells. Once inside the cell, the transgene can integrate into the host genome, allowing for the expression of the new trait in the resulting transgenic organism.

It is important to note that while transgenes can provide valuable insights and benefits in research and agriculture, their use and release into the environment are subjects of ongoing debate due to concerns about potential ecological impacts and human health risks.

This region of HsNV-2s genome has similarity to the INT_REC_C conserved domain. This domain is related to phage integrase and ... The C-terminal region of Hz2V008 has homology with the catalytic domain for integrase and recombinase, which has DNA breaking ... bacterial and yeast recombinase. It also contains motif cores for DNA binding sites, catalytic residues, the active sites, and ...
LR: 20150426; JID: 101285081; 0 (Bacterial Proteins); 0 (RNA, Ribosomal, 16S); EC 2.7.7.- (Rec A Recombinases); OID: NLM: ...
Rec A Protein. Rec A Recombinases. Receptor, Platelet-Derived-Growth Factor beta. Receptor, Platelet-Derived Growth Factor beta ...
Rec A Protein. Rec A Recombinases. Receptor, Platelet-Derived-Growth Factor beta. Receptor, Platelet-Derived Growth Factor beta ...
Rec A Protein. Rec A Recombinases. Receptor, Platelet-Derived-Growth Factor beta. Receptor, Platelet-Derived Growth Factor beta ...
Rec A Protein. Rec A Recombinases. Receptor, Platelet-Derived-Growth Factor beta. Receptor, Platelet-Derived Growth Factor beta ...
Rec A Protein. Rec A Recombinases. Receptor, Platelet-Derived-Growth Factor beta. Receptor, Platelet-Derived Growth Factor beta ...
Rec A Protein. Rec A Recombinases. Receptor, Platelet-Derived-Growth Factor beta. Receptor, Platelet-Derived Growth Factor beta ...
Rec A Protein. Rec A Recombinases. Receptor, Platelet-Derived-Growth Factor beta. Receptor, Platelet-Derived Growth Factor beta ...
Rec A Protein. Rec A Recombinases. Receptor, Platelet-Derived-Growth Factor beta. Receptor, Platelet-Derived Growth Factor beta ...
Rec A Protein. Rec A Recombinases. Receptor, Platelet-Derived-Growth Factor beta. Receptor, Platelet-Derived Growth Factor beta ...
Rec A Protein. Rec A Recombinases. Receptor, Platelet-Derived-Growth Factor beta. Receptor, Platelet-Derived Growth Factor beta ...
Rec A Protein. Rec A Recombinases. Receptor, Platelet-Derived-Growth Factor beta. Receptor, Platelet-Derived Growth Factor beta ...
Rec A Protein. Rec A Recombinases. Receptor, Platelet-Derived-Growth Factor beta. Receptor, Platelet-Derived Growth Factor beta ...
Rec A Recombinases Identity. PubMed Central ID * 16481492 Digital Object Identifier (DOI) * 10.1196/annals.1355.009 ...
Rad51 Recombinase. A Rec A recombinase found in eukaryotes. Rad51 is involved in DNA REPAIR of double-strand breaks.. ... GeneticGene DeletionNucleic Acid HybridizationRad51 RecombinaseChromosomes, Human, Pair 17Gonadal DisordersTetraploidyDNA ... PhosphoribosyltransferaseF-Box ProteinsFanconi Anemia Complementation Group F ProteinNeoplasm ProteinsRad51 RecombinaseDNA ...
Rec A Recombinases Medicine & Life Sciences 100% * Adenosine Triphosphate Medicine & Life Sciences 51% ...
Rec A Recombinases Medicine & Life Sciences 40% * Neoplasms Medicine & Life Sciences 36% ...
Rec A Recombinases * Escherichia coli K12 * DNA Helicases Explore _. Co-Authors (3) ...
Rec A Recombinases. *RNA Nucleotidyltransferases. *Sulfate Adenylyltransferase. *Transposases. *Transposon Resolvases. * ...
... the recombinase and primer form a protein/single-stranded nucleotide complex Rec/ssDNA, and invade the double-stranded DNA ... after finding the target region complementary to the primer and disintegration of the complex Rec/ssDNA, the polymerase also ...
Take a look at explain, for the first time, your operation of your microbe recombination technique utilizing beta-recombinase ... performing on half a dozen acknowledgement sequences (beta-rec/six) within N. crassa, which in turn permitted repetitive site- ...
Recombinase polymerase amplification (RPA) is an isothermal DNA amplification reaction at around 41 °C using recombinase (Rec ... Geobacillus , Recombinases , Recombinases/genética , Recombinases/metabolismo , DNA Polimerase Dirigida por DNA/genética , ... Recombinase polymerase amplification using novel thermostable strand-displacing DNA polymerases from Aeribacillus pallidus and ...
Rec A Recombinases. *Transposon Resolvases. *VDJ Recombinases. Below are MeSH descriptors whose meaning is more specific than " ... Recombinases involved in the rearrangement of immunity-related GENES such as IMMUNOGLOBULIN GENES and T-CELL RECEPTOR GENES. ... "VDJ Recombinases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ... This graph shows the total number of publications written about "VDJ Recombinases" by people in UAMS Profiles by year, and ...
Rec A Recombinases. *RNA Nucleotidyltransferases. *Sulfate Adenylyltransferase. *Transposases. *Transposon Resolvases. * ...
Rec A Recombinases [D08.811.913.696.445.692] * RNA Nucleotidyltransferases [D08.811.913.696.445.735] * Sulfate ...
Rec A Recombinases, SOS Response (Genetics). Abstract. BACKGROUND: Repairing DNA damage begins with its detection and is often ...
Press REC when you are done, to leave the recording mode.. Rainbow six siege aimbots. BLOG Trendline reports to track sales ... inducer of adipogenesis and prolonged nuclear translocation of Cre recombinase. He lives in another state and have not seem him ... These recreation activities that are beloved traditions for so many of us in New Mexico are also major drivers for our local ...

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