Amino Acyl-tRNA Synthetases: A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.RNA, Transfer, Amino Acyl: Intermediates in protein biosynthesis. The compounds are formed from amino acids, ATP and transfer RNA, a reaction catalyzed by aminoacyl tRNA synthetase. They are key compounds in the genetic translation process.Transfer RNA Aminoacylation: The conversion of uncharged TRANSFER RNA to AMINO ACYL TRNA.Isoleucine-tRNA Ligase: An enzyme that activates isoleucine with its specific transfer RNA. EC 6.1.1.5.Glycine-tRNA Ligase: An enzyme that activates glycine with its specific transfer RNA. EC 6.1.1.14.Alanine-tRNA Ligase: An enzyme that activates alanine with its specific transfer RNA. EC 6.1.1.7.Methionine-tRNA Ligase: An enzyme that activates methionine with its specific transfer RNA. EC 6.1.1.10.Tyrosine-tRNA Ligase: An enzyme that activates tyrosine with its specific transfer RNA. EC 6.1.1.1.RNA, Transfer: The small RNA molecules, 73-80 nucleotides long, that function during translation (TRANSLATION, GENETIC) to align AMINO ACIDS at the RIBOSOMES in a sequence determined by the mRNA (RNA, MESSENGER). There are about 30 different transfer RNAs. Each recognizes a specific CODON set on the mRNA through its own ANTICODON and as aminoacyl tRNAs (RNA, TRANSFER, AMINO ACYL), each carries a specific amino acid to the ribosome to add to the elongating peptide chains.Aminoacylation: A reaction that introduces an aminoacyl group to a molecule. TRANSFER RNA AMINOACYLATION is the first step in GENETIC TRANSLATION.Anticodon: The sequential set of three nucleotides in TRANSFER RNA that interacts with its complement in MESSENGER RNA, the CODON, during translation in the ribosome.Genetic Code: The meaning ascribed to the BASE SEQUENCE with respect to how it is translated into AMINO ACID SEQUENCE. The start, stop, and order of amino acids of a protein is specified by consecutive triplets of nucleotides called codons (CODON).Tryptophan-tRNA Ligase: An enzyme that activates tryptophan with its specific transfer RNA. EC 6.1.1.2.Molecular Sequence Data: 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.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.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Amino Acid Sequence: 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.Peptide Synthases: Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups.tRNA Methyltransferases: Enzymes that catalyze the S-adenosyl-L-methionine-dependent methylation of ribonucleotide bases within a transfer RNA molecule. EC 2.1.1.Lysine-tRNA Ligase: An enzyme that activates lysine with its specific transfer RNA. EC 6.1.1.6.Protein Biosynthesis: The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Leucine-tRNA Ligase: An enzyme that activates leucine with its specific transfer RNA. EC 6.1.1.4.Glutamate-tRNA Ligase: An enzyme that activates glutamic acid with its specific transfer RNA. EC 6.1.1.17.Serine-tRNA Ligase: An enzyme that activates serine with its specific transfer RNA. EC 6.1.1.11.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Sequence Alignment: 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.Valine-tRNA Ligase: An enzyme that activates valine with its specific transfer RNA. EC 6.1.1.9Phenylalanine-tRNA Ligase: An enzyme that activates phenylalanine with its specific transfer RNA. EC 6.1.1.20.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Aspartate-tRNA Ligase: An enzyme that activates aspartic acid with its specific transfer RNA. EC 6.1.1.12.Arginine-tRNA Ligase: An enzyme that activates arginine with its specific transfer RNA. EC 6.1.1.19.Protein Structure, Tertiary: 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.Histidine-tRNA Ligase: An enzyme that activates histidine with its specific transfer RNA. EC 6.1.1.21.Acylation: The addition of an organic acid radical into a molecule.Coenzyme A Ligases: Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.RNA, Transfer, Gln: A transfer RNA which is specific for carrying glutamine to sites on the ribosomes in preparation for protein synthesis.RNA, Transfer, Amino Acid-Specific: A group of transfer RNAs which are specific for carrying each one of the 20 amino acids to the ribosome in preparation for protein synthesis.RNA, Transfer, Ser: A transfer RNA which is specific for carrying serine to sites on the ribosomes in preparation for protein synthesis.Threonine-tRNA Ligase: An enzyme that activates threonine with its specific transfer RNA. EC 6.1.1.3.RNA, Transfer, Glu: A transfer RNA which is specific for carrying glutamic acid to sites on the ribosomes in preparation for protein synthesis.Acyl Coenzyme A: S-Acyl coenzyme A. Fatty acid coenzyme A derivatives that are involved in the biosynthesis and oxidation of fatty acids as well as in ceramide formation.RNA, Transfer, Gly: A transfer RNA which is specific for carrying glycine to sites on the ribosomes in preparation for protein synthesis.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Nucleic Acid Conformation: The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.RNA, Transfer, Pro: A transfer RNA which is specific for carrying proline to sites on the ribosomes in preparation for protein synthesis.RNA, Transfer, Ile: A transfer RNA which is specific for carrying isoleucine to sites on the ribosomes in preparation for protein synthesis.RNA, Transfer, Trp: A transfer RNA which is specific for carrying tryptophan to sites on the ribosomes in preparation for protein synthesis.Cloning, Molecular: 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.RNA, Transfer, Met: A transfer RNA which is specific for carrying methionine to sites on the ribosomes. During initiation of protein synthesis, tRNA(f)Met in prokaryotic cells and tRNA(i)Met in eukaryotic cells binds to the start codon (CODON, INITIATOR).Kinetics: The rate dynamics in chemical or physical systems.RNA, Transfer, Asp: A transfer RNA which is specific for carrying aspartic acid to sites on the ribosomes in preparation for protein synthesis.RNA, Transfer, Ala: A transfer RNA which is specific for carrying alanine to sites on the ribosomes in preparation for protein synthesis.RNA, Transfer, Phe: A transfer RNA which is specific for carrying phenylalanine to sites on the ribosomes in preparation for protein synthesis.Peptide Biosynthesis, Nucleic Acid-Independent: The enzymatic synthesis of PEPTIDES without an RNA template by processes that do not use the ribosomal apparatus (RIBOSOMES).Mutation: 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.RNA, Transfer, Cys: A transfer RNA which is specific for carrying cysteine to sites on the ribosomes in preparation for protein synthesis.RNA, Transfer, Arg: A transfer RNA which is specific for carrying arginine to sites on the ribosomes in preparation for protein synthesis.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.RNA, Bacterial: Ribonucleic acid in bacteria having regulatory and catalytic roles as well as involvement in protein synthesis.Codon: A set of three nucleotides in a protein coding sequence that specifies individual amino acids or a termination signal (CODON, TERMINATOR). Most codons are universal, but some organisms do not produce the transfer RNAs (RNA, TRANSFER) complementary to all codons. These codons are referred to as unassigned codons (CODONS, NONSENSE).RNA, Transfer, His: A transfer RNA which is specific for carrying histidine to sites on the ribosomes in preparation for protein synthesis.Bacterial Proteins: Proteins found in any species of bacterium.Amino Acid Substitution: The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.Isoleucine: An essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of LEUCINE. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.RNA, Transfer, Val: A transfer RNA which is specific for carrying valine to sites on the ribosomes in preparation for protein synthesis.Thermus thermophilus: A species of gram-negative, aerobic, rod-shaped bacteria found in hot springs of neutral to alkaline pH, as well as in hot-water heaters.Genes, Bacterial: The functional hereditary units of BACTERIA.Protein Conformation: 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).Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Ligases: A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.Evolution, Molecular: The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.Acyltransferases: Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (From Enzyme Nomenclature 1992) EC 2.3.Tyrocidine: An antibiotic mixture produced by Bacillus brevis which may be separated into three components, tyrocidines A, B, and C. It is the major constituent (40-60 per cent) of tyrothricin, gramicidin accounting for the remaining 10-20 per cent active material. It is a topical antimicrobial agent, that is very toxic parenterally.Pantetheine: An intermediate in the pathway of coenzyme A formation in mammalian liver and some microorganisms.Adenosine Monophosphate: Adenine nucleotide containing one phosphate group esterified to the sugar moiety in the 2'-, 3'-, or 5'-position.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Leucine: An essential branched-chain amino acid important for hemoglobin formation.Sequence Homology, Nucleic Acid: 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.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Acetate-CoA Ligase: An enzyme that catalyzes the formation of CoA derivatives from ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl CoA. It acts also on propionates and acrylates. EC 6.2.1.1.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.Species Specificity: The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Valine: A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.Protein Binding: 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.Molecular Weight: The sum of the weight of all the atoms in a molecule.Ribosomes: Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.Amino Acid Motifs: Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.Plasmids: 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.Methanobacteriaceae: A family of anaerobic, coccoid to rod-shaped METHANOBACTERIALES. Cell membranes are composed mainly of polyisoprenoid hydrocarbons ether-linked to glycerol. Its organisms are found in anaerobic habitats throughout nature.Thiolester HydrolasesRNA, Transfer, Asn: A transfer RNA which is specific for carrying asparagine to sites on the ribosomes in preparation for protein synthesis.Molecular Structure: The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.Multienzyme Complexes: Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.RNA, Fungal: Ribonucleic acid in fungi having regulatory and catalytic roles as well as involvement in protein synthesis.Multigene Family: 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)RNA Editing: A process that changes the nucleotide sequence of mRNA from that of the DNA template encoding it. Some major classes of RNA editing are as follows: 1, the conversion of cytosine to uracil in mRNA; 2, the addition of variable number of guanines at pre-determined sites; and 3, the addition and deletion of uracils, templated by guide-RNAs (RNA, GUIDE).Fatty Acids: Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed)Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Amide Synthases: Enzymes that catalyze the joining of either ammonia or an amide with another molecule, in which the linkage is in the form of a carbon-nitrogen bond. EC 6.3.1.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.Phenylalanine: An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.RNA, Transfer, Thr: A transfer RNA which is specific for carrying threonine to sites on the ribosomes in preparation for protein synthesis.Lysine: An essential amino acid. It is often added to animal feed.Restriction Mapping: Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.Suppression, Genetic: Mutation process that restores the wild-type PHENOTYPE in an organism possessing a mutationally altered GENOTYPE. The second "suppressor" mutation may be on a different gene, on the same gene but located at a distance from the site of the primary mutation, or in extrachromosomal genes (EXTRACHROMOSOMAL INHERITANCE).Geobacillus stearothermophilus: A species of GRAM-POSITIVE ENDOSPORE-FORMING BACTERIA in the family BACILLACEAE, found in soil, hot springs, Arctic waters, ocean sediments, and spoiled food products.Methanococcus: 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.Conserved Sequence: 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.Adenosine Triphosphate: 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.2',5'-Oligoadenylate Synthetase: An enzyme that catalyzes the conversion of ATP into a series of (2'-5') linked oligoadenylates and pyrophosphate in the presence of double-stranded RNA. These oligonucleotides activate an endoribonuclease (RNase L) which cleaves single-stranded RNA. Interferons can act as inducers of these reactions. EC 2.7.7.-.Amino Acids, Essential: Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Glutamate-Ammonia Ligase: An enzyme that catalyzes the conversion of ATP, L-glutamate, and NH3 to ADP, orthophosphate, and L-glutamine. It also acts more slowly on 4-methylene-L-glutamate. (From Enzyme Nomenclature, 1992) EC 6.3.1.2.Temperature: 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.DNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.RNA, Transfer, Leu: A transfer RNA which is specific for carrying leucine to sites on the ribosomes in preparation for protein synthesis.Genes: A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.RNA, Archaeal: Ribonucleic acid in archaea having regulatory and catalytic roles as well as involvement in protein synthesis.Coenzyme ASequence Analysis, DNA: A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.Thiouridine: A photoactivable URIDINE analog that is used as an affinity label.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.N-Acylneuraminate Cytidylyltransferase: An enzyme that forms CMP-acylneuraminic acids, which donate the N-acylneuraminic acid residues to the terminal sugar residue of a ganglioside or glycoprotein. EC 2.7.7.43.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Genetic Complementation Test: 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.Alanine: A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.RNA: A polynucleotide consisting essentially of chains with a repeating backbone of phosphate and ribose units to which nitrogenous bases are attached. RNA is unique among biological macromolecules in that it can encode genetic information, serve as an abundant structural component of cells, and also possesses catalytic activity. (Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Protein Structure, Secondary: 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.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.Mitochondria: Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)Streptomyces: A genus of bacteria that form a nonfragmented aerial mycelium. Many species have been identified with some being pathogenic. This genus is responsible for producing a majority of the ANTI-BACTERIAL AGENTS of practical value.Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Bacillus subtilis: A species of gram-positive bacteria that is a common soil and water saprophyte.RNA, Transfer, Tyr: A transfer RNA which is specific for carrying tyrosine to sites on the ribosomes in preparation for protein synthesis.Glutamine: A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.Open Reading Frames: 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).Genes, Fungal: The functional hereditary units of FUNGI.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Diphosphates: Inorganic salts of phosphoric acid that contain two phosphate groups.Amino Acid Transport Systems: Cellular proteins and protein complexes that transport amino acids across biological membranes.Yeasts: A general term for single-celled rounded fungi that reproduce by budding. Brewers' and bakers' yeasts are SACCHAROMYCES CEREVISIAE; therapeutic dried yeast is YEAST, DRIED.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Peptide Elongation Factor Tu: A protein found in bacteria and eukaryotic mitochondria which delivers aminoacyl-tRNA's to the A site of the ribosome. The aminoacyl-tRNA is first bound to a complex of elongation factor Tu containing a molecule of bound GTP. The resulting complex is then bound to the 70S initiation complex. Simultaneously the GTP is hydrolyzed and a Tu-GDP complex is released from the 70S ribosome. The Tu-GTP complex is regenerated from the Tu-GDP complex by the Ts elongation factor and GTP.Polyketide Synthases: Large enzyme complexes composed of a number of component enzymes that are found in STREPTOMYCES which biosynthesize MACROLIDES and other polyketides.Euglena: A genus of EUKARYOTES, in the phylum EUGLENIDA, found mostly in stagnant water. Characteristics include a pellicle usually marked by spiral or longitudinal striations.Chromatography, Thin Layer: Chromatography on thin layers of adsorbents rather than in columns. The adsorbent can be alumina, silica gel, silicates, charcoals, or cellulose. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Bacteria: 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.Mutagenesis: Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.Macromolecular Substances: Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.Stigmatella aurantiaca: A species of STIGMATELLA usually isolated from rotting wood. (From Bergey's Manual of Determinative Bacteriology, 9th ed)Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Methionine: A sulfur-containing essential L-amino acid that is important in many body functions.Genes, Suppressor: Genes that have a suppressor allele or suppressor mutation (SUPPRESSION, GENETIC) which cancels the effect of a previous mutation, enabling the wild-type phenotype to be maintained or partially restored. For example, amber suppressors cancel the effect of an AMBER NONSENSE MUTATION.Peptide Chain Elongation, Translational: A process of GENETIC TRANSLATION, when an amino acid is transferred from its cognate TRANSFER RNA to the lengthening chain of PEPTIDES.Tryptophan: An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.RNA Processing, Post-Transcriptional: Post-transcriptional biological modification of messenger, transfer, or ribosomal RNAs or their precursors. It includes cleavage, methylation, thiolation, isopentenylation, pseudouridine formation, conformational changes, and association with ribosomal protein.DNA, Bacterial: Deoxyribonucleic acid that makes up the genetic material of bacteria.Nitrogenous Group Transferases: Enzymes that catalyze the transfer of nitrogenous groups, primarily amino groups, from a donor, generally an amino acid, to an acceptor, usually a 2-oxoacid. EC 2.6.Archaeal Proteins: Proteins found in any species of archaeon.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Araliaceae: The ginseng plant family of the order Apiales, subclass Rosidae, class Magnoliopsida. Leaves are generally alternate, large, and compound. Flowers are five-parted and arranged in compound flat-topped umbels. The fruit is a berry or (rarely) a drupe (a one-seeded fruit). It is well known for plant preparations used as adaptogens (immune support and anti-fatigue).Eukaryotic Cells: Cells of the higher organisms, containing a true nucleus bounded by a nuclear membrane.Magnetic Resonance Spectroscopy: Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).Endoribonucleases: A family of enzymes that catalyze the endonucleolytic cleavage of RNA. It includes EC 3.1.26.-, EC 3.1.27.-, EC 3.1.30.-, and EC 3.1.31.-.Glycine: A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Saccharomyces cerevisiae Proteins: Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.DNA: 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).Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Magnesium: A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.Peptide Biosynthesis: The production of PEPTIDES or PROTEINS by the constituents of a living organism. The biosynthesis of proteins on RIBOSOMES following an RNA template is termed translation (TRANSLATION, GENETIC). There are other, non-ribosomal peptide biosynthesis (PEPTIDE BIOSYNTHESIS, NUCLEIC ACID-INDEPENDENT) mechanisms carried out by PEPTIDE SYNTHASES and PEPTIDYLTRANSFERASES. Further modifications of peptide chains yield functional peptide and protein molecules.Chromatography: Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts.Sequence Analysis: A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information.Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Biocatalysis: The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.Nucleoside Q: A modified nucleoside which is present in the first position of the anticodon of tRNA-tyrosine, tRNA-histidine, tRNA-asparagine and tRNA-aspartic acid of many organisms. It is believed to play a role in the regulatory function of tRNA. Nucleoside Q can be further modified to nucleoside Q*, which has a mannose or galactose moiety linked to position 4 of its cyclopentenediol moiety.Bacillus: A genus of BACILLACEAE that are spore-forming, rod-shaped cells. Most species are saprophytic soil forms with only a few species being pathogenic.Genes, Archaeal: The functional genetic units of ARCHAEA.Adenine NucleotidesChemistry: A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.Serine: A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.Fatty Acid Synthases: Enzymes that catalyze the synthesis of FATTY ACIDS from acetyl-CoA and malonyl-CoA derivatives.Chemical Phenomena: The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.Cell-Free System: A fractionated cell extract that maintains a biological function. A subcellular fraction isolated by ultracentrifugation or other separation techniques must first be isolated so that a process can be studied free from all of the complex side reactions that occur in a cell. The cell-free system is therefore widely used in cell biology. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p166)Plants: Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.Prokaryotic Cells: Cells lacking a nuclear membrane so that the nuclear material is either scattered in the cytoplasm or collected in a nucleoid region.EstersPeptides, Cyclic: Peptides whose amino and carboxy ends are linked together with a peptide bond forming a circular chain. Some of them are ANTI-INFECTIVE AGENTS. Some of them are biosynthesized non-ribosomally (PEPTIDE BIOSYNTHESIS, NON-RIBOSOMAL).Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing): An enzyme that catalyzes the formation of carbamoyl phosphate from ATP, carbon dioxide, and glutamine. This enzyme is important in the de novo biosynthesis of pyrimidines. EC 6.3.5.5.Stereoisomerism: The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Polymerase Chain Reaction: In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.Threonine: An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Oligoribonucleotides: A group of ribonucleotides (up to 12) in which the phosphate residues of each ribonucleotide act as bridges in forming diester linkages between the ribose moieties.

In vivo and in vitro processing of the Bacillus subtilis transcript coding for glutamyl-tRNA synthetase, serine acetyltransferase, and cysteinyl-tRNA synthetase. (1/1309)

In Bacillus subtilis, the adjacent genes gltX, cysE, and cysS encoding respectively glutamyl-tRNA synthetase, serine acetyl-transferase, and cysteinyl-tRNA synthetase, are transcribed as an operon but a gltX probe reveals only the presence of a monocistronic gltX mRNA (Gagnon et al., 1994, J Biol Chem 269:7473-7482). The transcript of the gltX-cysE intergenic region contains putative alternative secondary structures forming a p-independent terminator or an antiterminator, and a conserved sequence (T-box) found in the leader of most aminoacyl-tRNA synthetase and many amino acid biosynthesis genes in B. subtilis and in other Gram-positive eubacteria. The transcription of these genes is initiated 45 nt upstream from the first codon of gltX and is under the control of a sigmaA-type promoter. Analysis of the in vivo transcript of this operon revealed a cleavage site immediately downstream from the p-independent terminator structure. In vitro transcription analysis, using RNA polymerases from Escherichia coli, B. subtilis, and that encoded by the T7 phage, in the presence of various RNase inhibitors, shows the same cleavage. This processing generates mRNAs whose 5'-end half-lives differ by a factor of 2 in rich medium, and leaves putative secondary structures at the 3' end of the gltX transcript and at the 5' end of the cysE/S mRNA, which may be involved in the stabilization of these mRNAs. By its mechanism and its position, this cleavage differs from that of the other known transcripts encoding aminoacyl-tRNA synthetases in B. subtilis.  (+info)

The peculiar architectural framework of tRNASec is fully recognized by yeast AspRS. (2/1309)

The wild-type transcript of Escherichia coli tRNASec, characterized by a peculiar core architecture and a large variable region, was shown to be aspartylatable by yeast AspRS. Similar activities were found for tRNASec mutants with methionine, leucine, and tryptophan anticodons. The charging efficiency of these molecules was found comparable to that of a minihelix derived from tRNAAsp and is accounted for by the presence of the discriminator residue G73, which is a major aspartate identity determinant. Introducing the aspartate identity elements from the anticodon loop (G34, U35, C36, C38) into tRNASec transforms this molecule into an aspartate acceptor with kinetic properties identical to tRNAAsp. Expression of the aspartate identity set in tRNASec is independent of the size of its variable region. The functional study was completed by footprinting experiments with four different nucleases as structural probes. Protection patterns by AspRS of transplanted tRNASec and tRNAAsp were found similar. They are modified, particularly in the anticodon loop, upon changing the aspartate anticodon into that of methionine. Altogether, it appears that recognition of a tRNA by AspRS is more governed by the presence of the aspartate identity set than by the structural framework that carries this set.  (+info)

Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex. (3/1309)

Cytoplasmic aminoacyl-tRNA synthetases of higher eukaryotes acquired extra peptides in the course of their evolution. It has been thought that these appendices are related to the occurrence of the multiprotein complex consisting of at least eight different tRNA synthetase polypeptides. This complex is believed to be a signature feature of metazoans. In this study, we used multiple sequence alignments to infer the locations of the peptide appendices from human cytoplasmic tRNA synthetases found in the multisynthetase complex. The selected peptide appendices ranged from 22 aa of aspartyl-tRNA synthetase to 267 aa of methionyl-tRNA synthetase. We then made genetic constructions to investigate interactions between all 64 combinations of these peptides that were individually fused to nonsynthetase test proteins. The analyses identified 11 (10 heterologous and 1 homologous) interactions. The six peptide-dependent interactions paralleled what had been detected by crosslinking methods applied to the isolated multisynthetase complex. Thus, small peptide appendices seem to link together different synthetases into a complex. In addition, five interacting pairs that had not been detected previously were suggested from the observed peptide-dependent complexes.  (+info)

Immunoelectron microscopic localization of glutamyl-/ prolyl-tRNA synthetase within the eukaryotic multisynthetase complex. (4/1309)

A high molecular mass complex of aminoacyl-tRNA synthetases is readily isolated from a variety of eukaryotes. Although its composition is well characterized, knowledge of its structure and organization is still quite limited. This study uses antibodies directed against prolyl-tRNA synthetase for immunoelectron microscopic localization of the bifunctional glutamyl-/prolyl-tRNA synthetase. This is the first visualization of a specific site within the multisynthetase complex. Images of immunocomplexes are presented in the characteristic views of negatively stained multisynthetase complex from rabbit reticulocytes. As described in terms of a three domain working model of the structure, in "front" views of the particle and "intermediate" views, the primary antibody binding site is near the intersection between the "base" and one "arm." In "side" views, where the particle is rotated about its long axis, the binding site is near the midpoint. "Top" and "bottom" views, which appear as square projections, are also consistent with the central location of the binding site. These data place the glutamyl-/prolyl-tRNA synthetase polypeptide in a defined area of the particle, which encompasses portions of two domains, yet is consistent with the previous structural model.  (+info)

Ultrastructure of the eukaryotic aminoacyl-tRNA synthetase complex derived from two dimensional averaging and classification of negatively stained electron microscopic images. (5/1309)

Several aminoacyl-tRNA synthetases in higher eukaryotes are consistently isolated as a multi-enzyme complex for which little structural information is yet known. This study uses computational methods for analysis of electron microscopic images of the particle. A data set of almost 2000 negatively stained images was processed through reference-free alignment and multivariate statistical analysis. Interpretable structural information was evident in five eigenvectors. Hierarchical ascendant classification extracted clusters corresponding to distinct image orientations. The class averages are consistent with rotations around and orthogonal to a central particle axis and provide particle measurements: approximately 25 nm in height, 30 nm at the widest point and 23 nm thick. The results also provide objective evidence in support of the working structural model and demonstrate the feasibility of obtaining the three dimensional structure of the multisynthetase complex by single particle reconstruction methods.  (+info)

The identity determinants required for the discrimination between tRNAGlu and tRNAAsp by glutamyl-tRNA synthetase from Escherichia coli. (6/1309)

We previously elucidated the major determinant set for Escherichia coli tRNAGlu identity (U34, U35, C36, A37, G1*C72, U2*A71, U11*A24, U13*G22**Alpha46, and Delta47) and showed that the set is sufficient to switch the identity of tRNAGln to Glu [Sekine, S., Nureki, O., Sakamoto, K., Niimi, T., Tateno, M., Go, M., Kohno, T., Brisson, A., Lapointe, J. & Yokoyama, S. (1996) J. Mol. Biol. 256, 685-700]. In the present study, we attempted to switch the identity of tRNAAsp, which has a sequence similar to that of tRNAGlu, and consequently possesses many nucleotide residues corresponding to the Glu identity determinants (U35, C36, A37, G1*C72, and U11*A24). A simple transplantation of the rest of the major determinants (U34, U2*A71, U13*G22**Alpha46, and Delta47) to the framework of tRNAAsp did not result in a sufficient switch of the tRNAAsp identity to Glu. To confer an optimal glutamate accepting activity to tRNAAsp, two other elements, C4*G69 in the middle of the acceptor stem and C12*G23**C9 in the augmented D helix, were required. Consistently, the two base pairs, C4*G69 and C12*G23, in tRNAGlu had been shown to exist in the interface with glutamyl-tRNA synthetase (GluRS) by phosphate-group footprinting. We also found the two elements in the framework of tRNAGln, and determined that their contributions successfully changed the identity of tRNAGln to Glu in the previous study. By the identity-determinant set (C4*G69 and C12*G23**C9 in addition to U34, U35, C36, A37, G1*C72, U2*A71, U11*A24, U13*G22**Alpha46, and Delta47) the activity of GluRS was optimized and efficient discrimination from the noncognate tRNAs was achieved.  (+info)

tRNA synthetase mutants of Escherichia coli K-12 are resistant to the gyrase inhibitor novobiocin. (7/1309)

In previous studies we demonstrated that mutations in the genes cysB, cysE, and cls (nov) affect resistance of Escherichia coli to novobiocin (J. Rakonjac, M. Milic, and D. J. Savic, Mol. Gen. Genet. 228:307-311, 1991; R. Ivanisevic, M. Milic, D. Ajdic, J. Rakonjac, and D. J. Savic, J. Bacteriol. 177:1766-1771, 1995). In this work we expand this list with mutations in rpoN (the gene for RNA polymerase subunit sigma54) and the tRNA synthetase genes alaS, argS, ileS, and leuS. Similarly to resistance to the penicillin antibiotic mecillinam, resistance to novobiocin of tRNA synthetase mutants appears to depend upon the RelA-mediated stringent response. However, at this point the overlapping pathways of mecillinam and novobiocin resistance diverge. Under conditions of stringent response induction, either by the presence of tRNA synthetase mutations or by constitutive production of RelA protein, inactivation of the cls gene diminishes resistance to novobiocin but not to mecillinam.  (+info)

Progress toward the evolution of an organism with an expanded genetic code. (8/1309)

Several significant steps have been completed toward a general method for the site-specific incorporation of unnatural amino acids into proteins in vivo. An "orthogonal" suppressor tRNA was derived from Saccharomyces cerevisiae tRNA2Gln. This yeast orthogonal tRNA is not a substrate in vitro or in vivo for any Escherichia coli aminoacyl-tRNA synthetase, including E. coli glutaminyl-tRNA synthetase (GlnRS), yet functions with the E. coli translational machinery. Importantly, S. cerevisiae GlnRS aminoacylates the yeast orthogonal tRNA in vitro and in E. coli, but does not charge E. coli tRNAGln. This yeast-derived suppressor tRNA together with yeast GlnRS thus represents a completely orthogonal tRNA/synthetase pair in E. coli suitable for the delivery of unnatural amino acids into proteins in vivo. A general method was developed to select for mutant aminoacyl-tRNA synthetases capable of charging any ribosomally accepted molecule onto an orthogonal suppressor tRNA. Finally, a rapid nonradioactive screen for unnatural amino acid uptake was developed and applied to a collection of 138 amino acids. The majority of glutamine and glutamic acid analogs under examination were found to be uptaken by E. coli. Implications of these results are discussed.  (+info)

The aminoacyl-tRNA synthetases (EC 6.1.1.) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state, and have limited sequence homology. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric. Class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet fold flanked by alpha-helices, and are mostly dimeric or multimeric, containing at least three conserved regions. However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2-hydroxyl of the tRNA, while, in class II reactions, the 3-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, ...
The tRNA content and aminoacyl-tRNA synthetases of regenerating liver in the phase of rapid growth were compared with those of livers from both intact and sham-operated rats. At 48 h after hepatectomy, the amount of active tRNA (called total acceptor capacity) is significantly higher in regenerating liver than in control livers, owing to a general, possibly not uniform, increase in the various tRNA families, which suggests that it may contribute to the increased protein synthesis and to decreased protein degradation as well. The activities of most, but not of all, aminoacyl-tRNA synthetases in cell sap of regenerating liver tend to be greater than normal. Increased activity of histidyl-tRNA synthetase fits in with the possibility that the mechanisms that control the rate of protein degradation through aminoacylation of tRNAHis in cultured cells [Scornik (1983) J. Biol. Chem. 258, 882-886] also operate in the liver and play a role in regeneration. Sedimentation analysis of cell sap in sucrose ...
Aminoacyl‐tRNA synthetases (aaRSs) comprise an ancient, diverse enzyme family that catalyzes specific attachment of amino acids to their cognate tRNAs and ensures the accurate translation of the genetic code in the first step of protein synthesis (Carter, 1993; Martinis and Schimmel, 1996). The aminoacylation reaction is accomplished by a two‐step process: (a) activation of amino acids with ATP, forming aminoacyl adenylate, and (b) transfer of the aminoacyl residue to the 3′‐end of tRNA (Ibba and Söll, 2000). In this two‐step reaction, each tRNA synthetase molecule must select and activate its cognate amino acid from the cellular pool of 20 different proteinaceous amino acids. Because of the structural similarity of some amino acids, aaRSs really have difficulties in accurately discriminating cognate substrate from others (Baldwin and Berg, 1966; Loftfield and Vanderjagt, 1972). High fidelity in the amino‐acid selection process, which in some cases depends on hydrolytic editing to ...
Aminoacyl-tRNA synthetases are a group of enzymes which activate amino acids and transfer them to specific tRNA molecules as the first step in protein biosynthesis. In prokaryotic organisms there are at least twenty different types of aminoacyl-tRNA synthetases, one for each different amino acid. In eukaryotes there are generally two aminoacyl-tRNA synthetases for each different amino acid: one cytosolic form and a mitochondrial form ...
Why do ARSs form a complex? Channeling is clearly one possibility. Channeling has been suggested as an efficient way to utilize substrate for sequential reactions (Srere, 1987). For example, for sequential metabolic enzymes, stimulation of the first enzyme induced by a protein-protein interaction with the next provides a structural basis for channeling. The supramolecular assemblies of ARSs and elongation factors (Mirande, 1991; Kisselev and Wolfson, 1994; Yang, 1996) represent structural evidence for the subcellular organization of the protein synthesis machinery. Moreover, the existence of a channeled tRNA cycle during mammalian protein synthesis provides functional evidence for cellular compartmentalization of translation (Negrutskii and Deutscher, 1991; Negrutskii et al., 1994; Stapulionis and Deutscher, 1995). According to the proposed channeling scheme, aminoacyl-tRNAs are vectorially transferred from ARSs to ribosomes as ternary complexes of EF-1α, GTP and aminoacyl-tRNA (Negrutskii and ...
wrt-10 encodes a hedgehog-like protein, with an N-terminal signal sequence, a Wart domain, and a C-terminal region of low-complexity sequence. WRT-10 is expressed in both male and hermaphrodite intestine. the Wart domain is predicted to form a cysteine-crosslinked protein involved in intercellular signalling, and it has subtle similarity to the N-terminal Hedge domain of HEDGEHOG proteins. WRT-10 is required for normal growth to full size and locomotion. both of these requirements may reflect common defects in cholesterol-dependent hedgehog-like signalling or in vesicle trafficking. [Source: WormBase]wrt-10 encodes a hedgehog-like protein, with an N-terminal signal sequence, a Wart domain, and a C-terminal region of low-complexity sequence. WRT-10 is expressed in both male and hermaphrodite intestine. the Wart domain is predicted to form a cysteine-crosslinked protein involved in intercellular signalling, and it has subtle similarity to the N-terminal Hedge domain of HEDGEHOG proteins. WRT-10 is ...
Glutamyl-tRNA synthetase of Escherichia coli. Isolation and primary structure of the gltX gene and homology with other aminoacyl-tRNA synthetases. J. Biol. Chem. 261 (23), 10610-10617 (1986 ...
My group uses X-ray crystallography as a central technique to study the structure-function relationships of complexes involving RNA of various kinds in eukaryotic cells. This includes the transcription/replication machinery of segmented negative strand RNA viruses (e.g. influenza), complexes involved in sorting of Pol II transcripts into their appropriate processing pathways and innate immune system pattern recognition receptors, notably the response to viral RNA via Rig-I like helicases.. Keywords: Protein-RNA recognition / aminoacyl tRNA synthetases / RNA metabolism / virus structure / influenza virus polymerase / innate immunity / Rig-I like helicases / X-ray crystallography. Subject area(s): Microbiology, Virology & Pathogens , RNA , Structural Biology & Biophysics. ...
Accepted name: serine tRNA ligase. Reaction: ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer. Other name(s): seryl-tRNA synthetase; SerRS; seryl-transfer ribonucleate synthetase; seryl-transfer RNA synthetase; seryl-transfer ribonucleic acid synthetase; serine translase. Systematic name: L-serine:tRNASer ligase (AMP-forming). Comments: This enzyme also recognizes tRNASec, the special tRNA for selenocysteine, and catalyses the formation of L-seryl-tRNASec, the substrate for EC 2.9.1.1, L-seryl-tRNASec selenium transferase.. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9023-48-7. References:. 1. Katze, J.R. and Konigsberg, W. Purification and properties of seryl transfer ribonucleic acid synthetase from Escherichia coli. J. Biol. Chem. 245 (1970) 923-930. [PMID: 4906848]. 2. Makman, M.H. and Cantoni, G.L. Isolation of seryl and phenylalanyl ribonucleic acid synthetases from bakers yeast. Biochemistry 4 (1965) 1434-1442.. 3. Webster, L.T. and ...
Figure 1: A parallel genetic code. There are several major challenges in genetically encoding multiple unnatural amino acids into proteins in living cells. First, unique new codons are required that can be used to encode the incorporation of unnatural amino acids at specific sites in proteins. Since the 64 triplet codons are used in the genome of most organisms for encoding natural proteins additional codons (such as quadruplet codons) might be used to encode the incorporation of unnatural amino acids. Second, new aminoacyl-tRNA synthetase tRNA pairs that are orthogonal to the aminoacyl-tRNA synthetase/tRNA pairs in the host organism, and that uniquely direct the incorporation of an unnatural amino acid in response to a unique codon, are required. Finally the scope of cellular protein translation is limited to alpha-L amino acids and their close analogs, and alteration of the ribosome and potentially other components of the translational machinery are required to increase the chemical scope of ...
Background Aminoacyl-tRNA synthetases (AARSs) catalyze the first step of protein synthesis. We also established a strategy to check the natural activity of rhTyrRS by calculating aminoacylation and IL-8 launch in rhTyrRS-treated HL-60 cells. Conclusions The characterization of purified rhTyrRS indicated that proteins could be found in pharmacokinetic and pharmacodynamic research. and animal research could possibly be carried out to judge its toxic and pharmacologic results then. In this scholarly study, rhTyrRS was indicated at a higher level in and purified for potential preclinical testing. Strategies Cells and antibodies The skilled stress BL21 (F-ompT hsdS (rB-mB-) gal dcm; providded by aTyr Pharma) was utilized as the sponsor for rhTyrRS manifestation. This stress was transformed using the pET24a inducible manifestation vector where the His-tag series was deleted as well as the T7 promoter was changed having a Tac promoter. A mouse anti-human IL-8 monoclonal antibody ...
QARS, DARS, KARS. The current publication by Zhang and collaborators give us an interesting refresher course on basic molecular biology, particularly a section of the cellular machinery that I didnt believe to be relevant to human genetic epilepsies - tRNAs. In humans the amino acids are attached to the tRNAs through 37 different forms of tRNA synthetases, 17 of them only present in mitochondria. The names of the tRNA synthetases is derived from the specific amino acid symbol, followed by the suffix -ARS. Amongst the various tRNA synthetases implicated in human disease, two disease-related aaRS occur in a functional complex with QARS, the multisynthetase complex. These two aaRS are KARS and DARS. The KARS gene coding for the lysine tRNA synthetase has been found to be mutated in a particular form of Charcot-Marie-Tooth disease and, separately from this, nonsyndromic hearing loss. Mutations in the DARS gene coding for the asparate tRNA synthetase cause an inherited white matter disorder with leg ...
aminoacyl tRNA synthetase p18 component: shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1; amino acid sequence given in first source
... - reflects the multidimensional character of chemical biology, focusing in particular on the fundamental science of biological structures and systems, the use of chemical and biological techniques to elucidate
TY - JOUR. T1 - Signaling pathways for TNF production induced by human aminoacyl-tRNA synthetase-associating factor, p43. AU - Park, Heonyong. AU - Park, Sang Gyu. AU - Kim, Junghee. AU - Ko, Young Gyu. AU - Kim, Sunghoon. PY - 2002/11. Y1 - 2002/11. N2 - The p43 protein is associated with human macromolecular aminoacyl tRNA synthetase complex and secreted to up-regulate diverse proinflammatory genes including TNF. Here we focused on the p43-induced TNF production and determined its responsible signal pathway. The p43-induced TNF production was mediated by the activation of MAPK family members, ERK and p38 MAPK, and by IκB degradation leading to the activation of NFκB. We also studied the upstream molecules for ERK and p38 MAPK by using a variety of inhibitors. The inhibitors for protein kinase C (PKC) and phospholipase C (PLC) prevented the p43-induced TNF production. Interestingly, all of the effective drugs inhibited the ERK activity, while the drugs had no effects on p38 MAPK activity and ...
Eprs - mouse gene knockout kit via CRISPR, 1 kit. |dl||dt|Kit Component:|/dt||dd|- |strong|KN305300G1|/strong|, Eprs gRNA vector 1 in |a href=http://www.origene.com/CRISPR-CAS9/Detail.
Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation ...
We use cookies to ensure that we give you the best experience on our website. If you continue to use this site we will assume that you are happy with it.Ok ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Appropriate attachment of an amino acid to its cognate tRNA is the key to faithful translation of the genetic code. The family of enzymes responsible for this is the aminoacyl-tRNA synthetases (AATRSs) (EC 6.1.1.-). AATRSs catalyse a two-step reaction: (1) Enzyme + amino acid + ATP - Enzyme(aminoacyl-AMP) + PPi (2) tRNA + Enzyme(aminoacyl-AMP) - aminoacyl-tRNA + AMP + Enzyme In the first step, they form an aminoacyl-adenylate, in which the carboxyl of the amino acid is linked to the alpha-phosphate of ATP, by displacing the pyrophosphate. When the correct tRNA is bound, the aminoacyl group is transferred to the 2- or 3-terminal OH of the tRNA at the expense of AMP [1]. Based on structural and sequence comparisons, this group of at least 20 proteins (in prokaryotes there are approximately 20, but in eukaryotes there are usually 2 forms for each amino acid; namely, the cytosolic and mitochondrial forms) can be divided into two classes. Class I AATRSs contain a characteristic Rossman fold ...
Phylogenetic analysis of aminoacyl-tRNA synthetases (aaRSs) of all 20specificities from completely sequenced bacterial, archaeal, andeukaryotic genomes reveals a complex evolutionary picture. Detailedexamination of the domain architecture of aaRSs using sequence profilesearches delineated a network of partially conserved domains that is evenmore elaborate than previously suspected. Several unexpected evolutionaryconnections were identified, including the apparent origin of thebeta-subunit of bacterial GlyRS from the HD superfamily of hydrolases, adomain shared by bacterial AspRS and the B subunit of archaealglutamyl-tRNA amidotransferases, and another previously undetected domainthat is conserved in a subset of ThrRS, guanosine polyphosphate hydrolasesand synthetases, and a family of GTPases. Comparison of domainarchitectures and multiple alignments resulted in the delineation ofsynapomorphies-shared derived characters, such as extra domains orinserts-for most of the aaRSs specificities. These ...
Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with…
Leu-AMS (compound 6),亮氨酸类似物,是一种有效的亮氨酰-tRNA 合成酶 (LRS) 抑制剂,IC50 值为 22.34 nM,Leu-AMS 抑制了LRS 的催化活性,但不影响亮氨酸诱导的 mTORC1 活化。Leu-AMS在癌细胞和正常细胞中显示出细胞毒性,并抑制细菌的生长 ...
Semantic Scholar extracted view of [14C]erythromycin-ribosome complex formation and non-enzymatic binding of aminoacyl-transfer RNA to ribosome-messenger RNA complex. by Kohichi Tanaka et al.
Rabbit polyclonal Glutamyl Prolyl tRNA synthetase antibody validated for WB, IHC and tested in Human. With 4 independent reviews. Immunogen corresponding to…
Mouse monoclonal valyl tRNA synthetase antibody [VARSA7E6] validated for WB, Dot and tested in Human. Immunogen corresponding to recombinant fragment
Plasmid pDULE-ABK from Dr. Peter Schultzs lab contains the inserts tRNA synthetase and tRNA for a photocrosslinking amino acid and is published in Chembiochem. 2011 Aug 16;12(12):1854-7. doi: 10.1002/cbic.201100194. Epub 2011 Jun 15. This plasmid is available through Addgene.
Looking for online definition of aminoacyl-tRNA synthetases in the Medical Dictionary? aminoacyl-tRNA synthetases explanation free. What is aminoacyl-tRNA synthetases? Meaning of aminoacyl-tRNA synthetases medical term. What does aminoacyl-tRNA synthetases mean?
Histidyl-tRNA synthetase (HARS) also known as histidine-tRNA ligase, is an enzyme which in humans is encoded by the HARS gene. Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis. HARS has been shown to interact with EEF1B2 and EEF1G. GRCh38: Ensembl release 89: ENSG00000170445 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000001380 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". "Entrez Gene: HARS ...
Using fluorescent antibody staining, we have established the association of methionyl-tRNA synthetase with the endoplasmic reticulum in PtK2 cells. After Triton X-100 extraction, 70% of the recovered aminoacyl-tRNA synthetase activity was found in the detergent-insoluble fraction. This fraction of the enzyme remained localized with insoluble endoplasmic reticulum antigens and with ribosomes, which were stained with acridine orange. By both fluorescence microscopy and electron microscopy the organization of the detergent-insoluble residue was found to depend on the composition of the extracting solution. After extraction with a microtubule-stabilizing buffer containing EGTA, Triton X-100, and polyethylene glycol (Osburn, M., and K. Weber, 1977, Cell, 12:561-571) the ribosomes were aggregated in large clusters with remnants of membranes. After extraction with a buffer containing Triton X-100, sucrose, and CaCl2 (Fulton, A. B., K. M. Wang, and S. Penman, 1980, Cell, 20:849-857), the ribosomes were ...
Using fluorescent antibody staining, we have established the association of methionyl-tRNA synthetase with the endoplasmic reticulum in PtK2 cells. After Triton X-100 extraction, 70% of the recovered aminoacyl-tRNA synthetase activity was found in the detergent-insoluble fraction. This fraction of the enzyme remained localized with insoluble endoplasmic reticulum antigens and with ribosomes, which were stained with acridine orange. By both fluorescence microscopy and electron microscopy the organization of the detergent-insoluble residue was found to depend on the composition of the extracting solution. After extraction with a microtubule-stabilizing buffer containing EGTA, Triton X-100, and polyethylene glycol (Osburn, M., and K. Weber, 1977, Cell, 12:561-571) the ribosomes were aggregated in large clusters with remnants of membranes. After extraction with a buffer containing Triton X-100, sucrose, and CaCl2 (Fulton, A. B., K. M. Wang, and S. Penman, 1980, Cell, 20:849-857), the ribosomes were ...
TY - JOUR. T1 - Interaction between human tRNA synthetases involves repeated sequence elements. AU - Rho, Seung Bae. AU - Lee, Kyoung Hoa. AU - Kim, Jung Woo. AU - Shiba, Kiyotaka. AU - Jo, Yeong Joon. AU - Kim, Sunghoon. PY - 1996/9/17. Y1 - 1996/9/17. N2 - Aminoacyl-tRNA synthetases (tRNA synthetases) of higher eukaryotes form a multiprotein complex. Sequence elements that are responsible for the protein assembly were searched by using a yeast two-hybrid system. Human cytoplasmic isoleucyl-tRNA synthetase is a component of the multi-tRNA synthetase complex and it contains a unique C-terminal appendix. This part of the protein was used as bait to identify an interacting protein from a HeLa cDNA library. The selected sequence represented the internal 317 amino acids of human bifunctional (glutamyl- and prolyl-) tRNA synthetase, which is also known to be a component of the complex. Both the C-terminal appendix of the isoleucyl-tRNA synthetase and the internal region of bifunctional tRNA ...
The SRP9/14 heterodimer is the latest member of a growing family of small α/β RNA binding proteins examples of which are: the ribonucleoprotein (RNP) domain (Nagai et al., 1990; Oubridge et al., 1994); the double‐stranded RNA binding domain (dsRBD) (Farrandon et al., 1994; Bycroft et al., 1995; Kharrat et al., 1995); the K homology (KH) domain (Musco et al., 1996); the coat protein of bacteriophage MS2 (Valegård et al., 1990); the translational initiation factor IF3 (Biou et al., 1995); the S1 RNA binding domain (Bycroft et al., 1997); and many ribosomal proteins (Nagai, 1996). The RNP and KH domains, as well as several ribosomal proteins (Liljas and Garber, 1995), belong to the so‐called split α‐β‐α motif differing from the dsRBD, MS2 and SRP9/14 where the sheet is a β‐meander. In aminoacyl‐tRNA synthetases, a number of different tRNA anti‐codon binding modules have also been characterized (Cusack, 1995; Moras and Poterszman, 1996). Interestingly, RNA and DNA binding ...
In enzymology , a valine-tRNA ligase ( EC 6.1.1.9 ) is an enzyme that catalyzes the chemical reaction The 3 substrates of this enzyme are ATP , L-valine , and tRNA(Val) , whereas its 3 products are AMP , diphosphate , and L-valyl-tRNA(Val) . This enzyme belongs to the family of ligases , to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-valine:tRNAVal ligase (AMP-forming) . Other names in common use include valyl-tRNA synthetase , valyl-transfer ribonucleate synthetase , valyl-transfer RNA synthetase , valyl-transfer ribonucleic acid synthetase , valine transfer ribonucleate ligase , and valine translase . This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl-trna biosynthesis . Structural studies As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1GAX , 1IVS , 1IYW , 1WK9 , and 1WKA . See also VARS References Berg P, Bergmann FH, Ofengand
Build: Wed Jun 21 18:33:50 EDT 2017 (commit: 4a3b2dc). National Center for Advancing Translational Sciences (NCATS), 6701 Democracy Boulevard, Bethesda MD 20892-4874 • 301-435-0888. ...
This invention provides methods and compositions for incorporation of an unnatural amino acid into a peptide using an orthogonal aminoacyl tRNA synthetase/tRNA pair. In particular, an orthogonal pair
The rapid progress of research in the tRNA field and recent advances in the understanding of the molecular basis of specificity in tRNA: protein interactions make it necessary to have all of the accumulated information in an easily accessible form. The purpose of this book is to fulfill that need by providing an up-to-date account of all aspects of research on transfer RNA, including its structure, biosynthesis, and interactions with the many proteins involved in protein biosynthesis. Beginning with an historical account, the book covers a broad area of research on tRNA biosynthesis, the different functions of tRNA in the genetic decoding process, its association with many different proteins, and the emerging rules governing the specificity of their interactions. In view of the impressive progress made in the last few years, several of the chapters are devoted to discussion of aminoacyl-tRNA synthetase tRNA interactions. An appendix containing the structural formulae of all modified nucleosides found in
Aminoacyl-tRNA synthetases (aaRSs) are modular enzymes globally conserved in the three kingdoms of life. All catalyze the same two-step reaction, i.e., the attachment of a proteinogenic amino acid on their cognate tRNAs, thereby mediating the correct expression of the genetic code. In addition, some aaRSs acquired other functions beyond this key role in translation. Genomics and X-ray crystallography have revealed great structural diversity in aaRSs (e.g., in oligomery and modularity, in ranking into two distinct groups each subdivided in 3 subgroups, by additional domains appended on the catalytic modules). AaRSs show huge structural plasticity related to function and limited idiosyncrasies that are kingdom or even species specific (e.g., the presence in many Bacteria of non discriminating aaRSs compensating for the absence of one or two specific aaRSs, notably AsnRS and/or GlnRS). Diversity, as well, occurs in the mechanisms of aaRS gene regulation that are not conserved in evolution, notably ...
Complete information for CARS2 gene (Protein Coding), Cysteinyl-TRNA Synthetase 2, Mitochondrial, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
JUPITER, FL - For the past several years, Min Guo, an assistant professor at The Scripps Research Institute (TSRI), has focused on the intricate actions of an ancient family of catalytic enzymes that play a key role in translation, the process of producing proteins. These complex enzymes are a group of fundamental molecules that make building blocks for protein production. Present in every cell, these enzymes-known as aminoacyl-transfer RNA synthetases (tRNA synthetases)-select the proper amino acids and assign them to transfer RNAs to make a protein in the ribosome. As an essential step of determining the genetic code, tRNA synthetases have been around for billions of years. However, this essential part of the protein-making machine did not stop evolving. Now, in a new study published online ahead of print on November 15, 2012, by the journal Molecular Cell, Guo, Ehud Razin of The Institute for Medical Research Israel-Canada, and a large team of international scientists have shown that this ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
Glutamyl-prolyl-tRNA synthetase. (Aliases: AATS,GluProRS,Aa-tRNA-syn-glupro,ERS,AATs-GluPro,CG5394,GluRS,glutamyl-prolyl-tRNA synthetase,Aats-glu,p200,aminoacyl-tRNA synthetase,GluPro-RS,EPRS,Dmel\CG5394) ...
Mouse Monoclonal Anti-Tryptophanyl tRNA synthetase Antibody (3A12) [PE]. Validated: WB, ELISA, ICC/IF, IP. Tested Reactivity: Human. 100% Guaranteed.
Mouse Monoclonal Anti-Seryl tRNA synthetase Antibody (1H4) [DyLight 488]. Validated: WB, ELISA, ICC/IF, IHC, IHC-P. Tested Reactivity: Human. 100% Guaranteed.
Adenosine monophosphate (AMP) is a key cellular metabolite regulating energy homeostasis and signal transduction. AMP is also a product of various enzymatic reactions, many of which are dysregulated during disease conditions. Thus, monitoring the activities of these enzymes is a primary goal for developing modulators for these enzymes. In this study, we demonstrate the versatility of an enzyme-coupled assay that quantifies the amount of AMP produced by any enzymatic reaction regardless of its substrates. We successfully implemented it to enzyme reactions that use adenosine triphosphate (ATP) as a substrate (aminoacyl tRNA synthetase and DNA ligase) by an elaborate strategy of removing residual ATP and converting AMP produced into ATP; so it can be detected using luciferase/luciferin and generating light ...
Article{pmid25409537, Author=Thibodeaux, C. J. and Ha, T. and van der Donk, W. A. , Title={{A} price to pay for relaxed substrate specificity: a comparative kinetic analysis of the class {I}{I} lanthipeptide synthetases {P}roc{M} and {H}al{M}2}, Journal=J. Am. Chem. Soc., Year=2014, Volume=136, Number=50, Pages=17513--17529, Month=Dec ...
Antibodies for proteins involved in ligase activity, forming aminoacyl-tRNA and related compounds pathways, according to their Panther/Gene Ontology Classification
K.NAKANISHI,Y.OGISO,T.NAKAMA,S.FUKAI,O.NUREKI. CRYSTAL STRUCTURE OF AQUIFEX AEOLICUS METHIONYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(MET) AND METHIONYL-ADENYLATE ANOLOGUE. TO BE PUBLISHED ...
July 15 2017 Issue The semi-monthly AARS online Hot Topics Newsletter is an exclusive AARS member benefit! You dont need to spend countless hours perusing your typical online sources when you have this! Stay informed today by becoming an AARS member and receiving the Hot Topics!
引用Abcams Anti-Glutamine Synthetase抗体(ab16802)的参考文献列表。为您列举引用本产品的发表文章,并提供信息包括论文文献数据库中的检索编号以便您搜寻文章
Aminoacyl-tRNA synthetase enzymes consume ATP in the attachment tRNA to amino acids, forming aminoacyl-tRNA complexes. ... Dozens of ATP equivalents are generated by the beta-oxidation of a single long acyl chain. The acetyl-CoA produced by beta- ... Aminoacyl transferase binds AMP-amino acid to tRNA. The coupling reaction proceeds in two steps: aa + ATP --> aa-AMP + PPi aa- ... AMP + tRNA --> aa-tRNA + AMP The amino acid is coupled to the penultimate nucleotide at the 3′-end of the tRNA (the A in the ...
This aminoacyl-tRNA precursor is produced in an ATP-dependent reaction carried out by an aminoacyl tRNA synthetase. This ... The acyl chains in the fatty acids are extended by a cycle of reactions that add the acyl group, reduce it to an alcohol, ... lack all amino acid synthesis and take their amino acids directly from their hosts. All amino acids are synthesized from ... 855-6. ISBN 0-7216-0240-1. Ibba M, Söll D (2001). "The renaissance of aminoacyl-tRNA synthesis". EMBO Rep. 2 (5): 382-7. doi: ...
This is accomplished by screening libraries of mutant amino acyl tRNA synthetases for mutants which charge nonsense-codon tRNAs ... The organism which expresses such a synthetase can then be genetically programmed to incorporate the unnatural amino acid into ... Normally, the unnatural amino acid itself must be synthesized in the lab and supplied to the organism by adding it to the ... The unnatural amino acid must also be able to pass through the organism's cell membrane into the interior of the organism. More ...
These are exemplified by work on amino acyl tRNA synthetases, crucial to protein synthesis in all living organisms and analyses ... Thermophilus seryl-tRNA synthetase complexed with tRNA(Ser)". Science. New York, N.Y. 263 (5152): 1404-10. doi:10.1126/science. ... "A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å". Nature. ...
... transfer RNA and amino-acyl-tRNA synthetases in mimiviruses. Intervirology 56(6):364-375. doi: 10.1159/000354557 Morgan Gaia et ... Virus Res 117(1):145-155 Colson P, Fournous G, Diene SM, Raoult D (2013) Codon usage, amino acid usage, ...
... amino acyl-trna synthetases MeSH D08.811.464.263.200.050 --- alanine-tRNA ligase MeSH D08.811.464.263.200.100 --- arginine-tRNA ... isoleucine-trna ligase MeSH D08.811.464.263.200.500 --- leucine-trna ligase MeSH D08.811.464.263.200.550 --- lysine-trna ligase ... glutamate-trna ligase MeSH D08.811.464.263.200.350 --- glycine-trna ligase MeSH D08.811.464.263.200.400 --- histidine-trna ... phenylalanine-trna ligase MeSH D08.811.464.263.200.750 --- serine-trna ligase MeSH D08.811.464.263.200.800 --- threonine-tRNA ...
Aminoacyl-tRNA synthetase enzymes consume ATP in the attachment tRNA to amino acids, forming aminoacyl-tRNA complexes. ... Dozens of ATP equivalents are generated by the beta-oxidation of a single long acyl chain.[20] The acetyl-CoA produced by beta- ... aa-AMP + tRNA --, aa-tRNA + AMP. The amino acid is coupled to the penultimate nucleotide at the 3′-end of the tRNA (the A in ... Amino acid activation in protein synthesisEdit. Main article: Amino acid activation ...
Amino Acyl-tRNA Synthetases at the US National Library of Medicine Medical Subject Headings (MeSH) AARS human gene location in ... An aminoacyl tRNA synthetase (aaRS) is an enzyme that attaches the appropriate amino acid onto its tRNA. It does so by ... In humans, the 21 different types of aa-tRNA are made by the 21 different aminoacyl-tRNA synthetases, one for each amino acid ... TARS (gene) "tRNA Synthetases". Retrieved 2007-08-18. "Molecule of the Month: Aminoacyl-tRNA Synthetases High Fidelity". ...
VARS Berg P, Bergmann FH, Ofengand EJ, Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid ... Other names in common use include valyl-tRNA synthetase, valyl-transfer ribonucleate synthetase, valyl-transfer RNA synthetase ... Bergmann FH, Berg P, Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid II. The ... This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl-trna biosynthesis. As of late 2007, 5 ...
Bergmann FH, Berg P, Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid II. The ... effects of coupling mutations in the acceptor stem on recognition of tRNAs by Escherichia coli Met-tRNA synthetase and Met-tRNA ... Other names in common use include methionyl-tRNA synthetase, methionyl-transfer ribonucleic acid synthetase, methionyl-transfer ... This enzyme participates in 3 metabolic pathways: methionine metabolism, selenoamino acid metabolism, and aminoacyl-trna ...
Berg P, Bergmann FH, Ofengand EJ, Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid I. ... isoleucyl-transfer RNA synthetase, isoleucine-transfer RNA ligase, isoleucine-tRNA synthetase, and isoleucine translase. This ... Other names in common use include isoleucyl-tRNA synthetase, isoleucyl-transfer ribonucleate synthetase, ... Bergmann FH, Berg P, Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid II. The ...
Leucyl-tRNA synthetase ALLEN EH, GLASSMAN E, SCHWEET RS (1960). "Incorporation of amino acids into ribonucleic acid. I. The ... Berg P, Bergmann FH, Ofengand EJ & Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid I. ... leucyl-transfer RNA synthetase, leucyl-transfer ribonucleic acid synthetase, leucine-tRNA synthetase, and leucine translase. ... Other names in common use include leucyl-tRNA synthetase, leucyl-transfer ribonucleate synthetase, ...
Aminoacyl-tRNA synthetases that mispair tRNAs with the wrong amino acids can produce mischarged aminoacyl-tRNAs, which can ... The correct amino acid is covalently bonded to the correct transfer RNA (tRNA) by amino acyl transferases. The amino acid is ... Aminoacyl tRNA synthetases (enzymes) catalyze the bonding between specific tRNAs and the amino acids that their anticodon ... The tRNA in the E site leaves and another aminoacyl-tRNA enters the A site to repeat the process. After the new amino acid is ...
Amino acid transporter. *Aminoacyl tRNA synthetases, class I. *Aminoacyl tRNA synthetases, class II ... Acyl-CoA:lysocardiolipin acyltransferase-1. *Acyl-protein thioesterase. *Acylphosphatase. *Acyltransferase like 2 ...
SARS belongs to the class II amino-acyl tRNA family and is found in all humans; its encoded enzyme, seryl-tRNA synthetase, is ... function and evolution of seryl-tRNA synthetases: implications for the evolution of aminoacyl-tRNA synthetases and the genetic ... function and evolution of seryl-tRNA synthetases: implications for the evolution of aminoacyl-tRNA synthetases and the genetic ... Heckl M, Busch K, Gross HJ (May 1998). "Minimal tRNA(Ser) and tRNA(Sec) substrates for human seryl-tRNA synthetase: ...
This reaction, called tRNA charging, is catalyzed by aminoacyl tRNA synthetase. A specific tRNA synthetase is responsible for ... Succinyl-diaminopimelate desuccinylase catalyzes the removal of acyl group from N-succinyl-L,L-diaminopimelic acid to yield L,L ... Aminoacyl − AMP + tRNA ↽ − − ⇀ aminoacyltRNA + AMP {\displaystyle {\ce {{Aminoacyl-AMP}+ tRNA <=> {aminoacyl-tRNA}+ AMP}}} ... both of which are catalyzed by aminoacyl tRNA synthetase, produces a charged tRNA that is ready to add amino acids to the ...
... effects of coupling mutations in the acceptor stem on recognition of tRNAs by Escherichia coli Met-tRNA synthetase and Met-tRNA ... Bergmann, F.H., Berg, P. and Dieckmann, M. (1961). „The enzymic synthesis of amino acyl derivatives of ribonucleic acid. II. ... The preparation of leucyl-, valyl-, isoleucyl- and methionyl ribonucleic acid synthetases from Escherichia coli". J. Biol. Chem ...
Further, this category also differentiates between amino-acyl and non-amino-acyl groups. Peptidyl transferase is a ribozyme ... it catalyzes the transfer of a peptide to an aminoacyl-tRNA, following this reaction: peptidyl-tRNAA + aminoacyl-tRNAB ⇌ {\ ... Fitzgerald DK, Brodbeck U, Kiyosawa I, Mawal R, Colvin B, Ebner KE (Apr 1970). "Alpha-lactalbumin and the lactose synthetase ... The transfer involves the removal of the growing amino acid chain from the tRNA molecule in the A-site of the ribosome and its ...
2.3.1: other than amino-acyl groups. *acetyltransferases: Acetyl-Coenzyme A acetyltransferase ... transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer. • citrate (Si)-synthase activity ... Citrate synthase has three key amino acids in its active site (known as the catalytic triad) which catalyze the conversion of ... Citrate synthase's 437 amino acid residues are organized into two main subunits, each consisting of 20 alpha-helices. These ...
This is followed by Cβ-Cγ bond cleavage to generate an acyl-enzyme intermediate together with a tautomerized Ala-PLP adduct. ... Forty percent of the amino acids are arranged in an alpha helical and twelve percent are arranged in beta sheets. Docking of ... cysteine+glutamate→glutathione: Gamma-glutamylcysteine synthetase. *Glutathione synthetase. *Gamma-glutamyl transpeptidase. * ...
Uridine monophosphate synthetase (EC 4.1.1.23). *Aromatic-L-amino-acid decarboxylase (EC 4.1.1.28) ... EC 2.9.1.2: O-phospho-L-seryl-tRNA(Sec):L-selenocysteinyl-tRNA synthase ... EC 6.2.1.20: [[Long-chain-fatty-acid--[acyl-carrier-protein] ligase]]. *EC 6.2.1.21: Transferred entry: 6.2.1.30 ... EC 2.8.1.15: tRNA-5-methyluridine(54) 2-sulfurtransferase. Category:EC 2.9 (transfer selenium-containing groups)Edit. *EC 2.9. ...
Molecular Characterization of a Major Plastidial Acyl-Coenzyme a Synthetase from Arabidopsis". Plant Physiology. 129 (4): 1700- ... Amino acid synthesis. Chloroplasts alone make almost all of a plant cell's amino acids in their stroma[158] except the sulfur- ... A few chloroplast genes found new homes in the mitochondrial genome-most became nonfunctional pseudogenes, though a few tRNA ... Fatty acid synthase (FAS) is a large complex of enzymes and cofactors including acyl carrier protein (ACP) which holds the acyl ...
A proposed mode of action of pseudomonic acid as an inhibitor of isoleucyl-tRNA synthetase". J. Biol. Chem. 269 (39): 24304-9. ... In E. coli IleRS, a single amino acid mutation was shown to alter mupirocin resistance. MuH is linked to the acquisition of a ... The mupirocin pathway also contains several tandem acyl carrier protein doublets or triplets. This may be an adaptation to ... Yanagisawa T, Lee JT, Wu HC, Kawakami M (September 1994). "Relationship of protein structure of isoleucyl-tRNA synthetase with ...
EC 6.1.1.1: tyrosine-tRNA ligase EC 6.1.1.2: tryptophan-tRNA ligase EC 6.1.1.3: threonine-tRNA ligase EC 6.1.1.4: leucine-tRNA ... acyl-carrier-protein) ligase EC 6.2.1.21: Covered by EC 6.2.1.30 EC 6.2.1.22: (citrate (pro-3S)-lyase) ligase EC 6.2.1.23: ... 5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase EC 6.3.2.27: The activity is covered by two independent enzymes, EC ... indoleacetate-lysine synthetase EC 6.3.2.21: ubiquitin-calmodulin ligase EC 6.3.2.22: Now EC 6.3.1.14 EC 6.3.2.23: ...
β-Oxidation uses pyruvate carboxylase, Acyl-CoA dehydrogenase, and 𝛽-Ketothiolase. Amino acid production is facilitated by ... Succinyl-CoA Synthetase, Fumarase, and Malate dehydrogenase. The Urea Cycle is facilitated by Carbamoyl phosphate synthetase I ... Protein synthesis makes use of mitochondrial DNA, RNA, and tRNA. Regulation of processes makes use of ions(Ca2+/K+/Mg+). ... These amino acids are then used either within the matrix or transported into the cytosol to produce proteins. Regulation within ...
Amino+Acyl-tRNA+Synthetases at the US National Library of Medicine Medical Subject Headings (MeSH) ... "Aminoacyl-tRNA synthetases". Structural Biology. 5: 48-55.. *^ "Molecule of the Month: Aminoacyl-tRNA Synthetases High Fidelity ... An aminoacyl-tRNA synthetase (aaRS or ARS), also called tRNA-ligase, is an enzyme that attaches the appropriate amino acid onto ... Amino Acid + tRNA + ATP → Aminoacyl-tRNA + AMP + PPi. Some synthetases also mediate an editing reaction to ensure high fidelity ...
Amino Acyl-tRNA Synthetases/genetics*. *Amino Acyl-tRNA Synthetases/metabolism. *Brain Diseases, Metabolic/enzymology ... Mitochondrial aminoacyl-tRNA synthetases in human disease.. Konovalova S1, Tyynismaa H. ... Mitochondrial aminoacyl-tRNA synthetases (mtARSs) are essential in the process of transferring genetic information from ... These synthetases perform an integral step in the initiation of mitochondrial protein synthesis by charging tRNAs with their ...
An aminoacyl tRNA synthetase (aaRS) is an enzyme that catalyzes the esterification of a specific amino acid or its precursor ... Aminoacyl tRNA synthetase. 6.2 - Carbon-Sulfur. Succinyl coenzyme A synthetase - Acetyl Co-A synthetase - Long fatty acyl CoA ... An aminoacyl tRNA synthetase (aaRS) is an enzyme that catalyzes the esterification of a specific amino acid or its precursor to ... Sum of 1 and 2: amino acid + tRNA + ATP → aminoacyl-tRNA + AMP + PPi ...
Amino Acyl-tRNA Synthetases/genetics. *Amino Acyl-tRNA Synthetases/metabolism*. *Biological Transport/genetics ... Import of tRNAs and aminoacyl-tRNA synthetases into mitochondria.. Duchêne AM1, Pujol C, Maréchal-Drouard L. ... All mitochondrial aminoacyl-tRNA synthetases and many tRNAs are imported from the cytosol into the mitochondria in eukaryotic ... Two crucial partners of the mitochondrial translation machinery are the aminoacyl-tRNA synthetases and the tRNAs. ...
Prolyl Amino-acyl tRNA SynthetaseImported. ,p>Information which has been imported from another database using automatic ... tr,O45869,O45869_CAEEL Prolyl Amino-acyl tRNA Synthetase OS=Caenorhabditis elegans GN=pars-2 PE=1 SV=1 ... Aminoacyl-tRNA synthetaseImported. ,p>Information which has been imported from another database using automatic procedures.,/p ... IPR002314. aa-tRNA-synt_IIb. IPR006195. aa-tRNA-synth_II. IPR004154. Anticodon-bd. IPR036621. Anticodon-bd_dom_sf. IPR002316. ...
Cysteinyl Amino-acyl tRNA SynthetaseImported. ,p>Information which has been imported from another database using automatic ... tr,A0A061ACL3,A0A061ACL3_CAEEL Cysteinyl Amino-acyl tRNA Synthetase OS=Caenorhabditis elegans OX=6239 GN=cars-1 PE=1 SV=1 ... Aminoacyl-tRNA synthetaseImported. ,p>Information which has been imported from another database using automatic procedures.,/p ... IPR015803 Cys-tRNA-ligase. IPR024909 Cys-tRNA/MSH_ligase. IPR032678 tRNA-synt_1_cat_dom. IPR009080 tRNAsynth_Ia_anticodon-bd. ...
First, the N-acyl O-aminopropylphosphoramidate linker of the aspartyl-adenylate moiety of processed McC (compound 2) was ... Aminoacyl-tRNA synthetases (aaRSs) carry out the condensation of genetically encoded amino acids with cognate tRNAs. When 1 of ... Synthetic Microcin C Analogs Targeting Different Aminoacyl-tRNA Synthetases. Pieter Van de Vijver, Gaston H. M. Vondenhoff, ... Synthetic Microcin C Analogs Targeting Different Aminoacyl-tRNA Synthetases. Pieter Van de Vijver, Gaston H. M. Vondenhoff, ...
Amino Acyl-tRNA Synthetases / antagonists & inhibitors* * Amino Acyl-tRNA Synthetases / metabolism* * Anti-Bacterial Agents / ... Aminoacyl-tRNA synthetases and their inhibitors as a novel family of antibiotics Appl Microbiol Biotechnol. 2003 May;61(4):278- ... In this regard, aminoacyl-tRNA synthetases (ARSs) provide a promising platform to develop novel antibiotics that show no cross- ...
aminoacyl tRNA synthetase p18 component: shares a protein motif with the beta and gamma subunits of eukaryotic elongation ... factor 1; amino acid sequence given in first source ... Amino Acyl-tRNA Synthetases: 128*aminoacyl tRNA synthetase p18 ... aminoacyl tRNA synthetase p18 component. Subscribe to New Research on aminoacyl tRNA synthetase p18 component ... shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1; amino acid sequence given in first ...
What is aminoacyl-tRNA synthetases? Meaning of aminoacyl-tRNA synthetases medical term. What does aminoacyl-tRNA synthetases ... Looking for online definition of aminoacyl-tRNA synthetases in the Medical Dictionary? aminoacyl-tRNA synthetases explanation ... aminoacyl-tRNA synthetases. Also found in: Dictionary, Thesaurus. a·mi·no·ac·yl-tRNA syn·the·tas·es. enzymes catalyzing the ... aminoacyl-tRNA. transfer RNA to which its specific amino acid has been coupled by its specific aminoacyl-tRNA synthetase. ...
M. barkeri encodes a special amber suppressor tRNA (tRNA(Pyl)) that presumably recog … ... the 22nd cotranslationally inserted amino acid, was found in the Methanosarcina barkeri monomethylamine methyltransferase ... Amino Acyl-tRNA Synthetases / metabolism *. Actions. * Search in PubMed * Search in MeSH ... We show that PylS is a specialized aminoacyl-tRNA synthetase for charging pyrrolysine to tRNA(Pyl); lysine and tRNA(Lys) are ...
Anti-synthetase syndrome is an autoimmune disease characterized by autoantibodies toward amino acyl-tRNA synthetases (ARS), ... Anti-synthetase syndrome is an autoimmune disease characterized by autoantibodies toward amino acyl-tRNA synthetases (ARS), ... Anti-aminoacyl-tRNA synthetase-related myositis and dermatomyositis: clues for differential diagnosis on muscle biopsy. *Bruna ... Cerbelli, B., Pisano, A., Colafrancesco, S. et al. Anti-aminoacyl-tRNA synthetase-related myositis and dermatomyositis: clues ...
dual targeting; amino acyl-tRNA synthetase; mitochondria; chloroplast; targeting peptide Identifiers. URN: urn:nbn:se:su:diva- ... Defining the Determinants for Dual Targeting of Amino Acyl-tRNA Synthetases to Mitochondria and Chloroplasts. Berglund, Anna- ... Most of the organellar amino acyl-tRNA synthetases (aaRSs) are dually targeted to both mitochondria and chloroplasts using dual ... as revealed by spectroscopic studies of a dTP of an aminoacyl- tRNA-synthetase (aaRS). In vitro and in vivo import experiments ...
... tRNA) and amino acyl-tRNA synthetases. We confirmed that the codon and amino acid usages of these giant viruses are highly ... Codon usage, amino acid usage, transfer RNA and amino-acyl-tRNA synthetases in mimiviruses ... We further describe that the set of tRNAs and amino acyl-tRNA synthetases in mimiviruses is globally not adapted to the codon ... Colson P., Fournous G., Diene S. M., Raoult Didier. (2013). Codon usage, amino acid usage, transfer RNA and amino-acyl-tRNA ...
Signaling pathways for TNF production induced by human aminoacyl-tRNA synthetase-associating factor, p43. In: Cytokine. 2002 ; ... Signaling pathways for TNF production induced by human aminoacyl-tRNA synthetase-associating factor, p43. Cytokine. 2002 Nov;20 ... The p43 protein is associated with human macromolecular aminoacyl tRNA synthetase complex and secreted to up-regulate diverse ... Signaling pathways for TNF production induced by human aminoacyl-tRNA synthetase-associating factor, p43. / Park, Heonyong; ...
acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase. New_papain: novel family of papain-like cysteine proteases - ... tyrosine-tRNA synthetase. WTRS: tryptophan-tRNA synthetase. Gene and protein abbreviations: 2OGFEDO: 2-oxoglutarate and iron(II ... The least studied of these systems are those utilizing tRNAs or aminoacyl-tRNA synthetases (AAtRS) in non-ribosomal peptide ... tRNAs charged with the cognate amino acids by lysyl- or alanyl-tRNA synthetases are used by bacterial enzymes typified by ...
... are enzymes that join amino acids to tRNAs. Although they are housekeeping enzymes essential for protein synthesis, aaRSs are ... These investigations will undoubtedly provide some of the most fundamental understanding of how and possibly why synthetases ... Amino Acyl-tRNA Synthetases, Animals, Humans, Protein Biosynthesis, RNA, Transfer, Amino Acid-Specific, Signal Transduction ... Aminoacyl-tRNA synthetases (aaRSs) are enzymes that join amino acids to tRNAs. Although they are housekeeping enzymes essential ...
Tyrosyl-tRNA synthetase: the first crystallization of a human mitochondrial amino-acyl-tRNA synthetase. ... Crystals of human mitochondrial tyrosyl-tRNA synthetase lacking the C-terminal S4-like domain diffract to 2.7 Å resolution and ...
Amino Acyl-tRNA Synthetases/genetics*. *Asian Continental Ancestry Group/genetics*. *Ethnic Groups/genetics* ... Aminoacyl-tRNA synthetases (ARSs) are in charge of cellular protein synthesis and have additional domains that function in a ... Association of aminoacyl-tRNA synthetases gene polymorphisms with the risk of congenital heart disease in the Chinese Han ... Association of Aminoacyl-tRNA Synthetases Gene Polymorphisms with the Risk of Congenital Heart Disease in the Chinese Han ...
Amino Acyl-tRNA Synthetases, Bacteria, Genomics, Phylogeny. Abstract. During their extended evolution genes coding for ... Application to aminoacyl-tRNA synthetase-like proteins.. Title. A genomics method to identify pathogenicity-related proteins. ... The ARS-related proteins that have resulted from these genetic events are generally known as aminoacyl-tRNA synthetase-like ... aminoacyl-tRNA synthetases (ARS) have experienced numerous instances of duplication, insertion and deletion of domains. ...
Aminoacyl-tRNA Synthetase 6.2.1.1 S-Acetyl Coenzyme A Synthetase 6.2.1.3 Acyl Coenzyme A Synthetase ...
0 (Multiprotein Complexes); 9014-25-9 (RNA, Transfer); EC 6.1.1.- (Amino Acyl-tRNA Synthetases). ... Survey of the transcriptome suggests recognition of the mitochondrial tRNA-Met by the cytoplasmic aminoacyl-tRNA synthetase ... Aminoacil-tRNA Sintetases/gen tica. Animais. Sequ ncia de Bases. Cubomedusas/metabolismo. Regula o da Express o G nica. Genes ... counterpart and C-to-U editing of the cytoplasmic tRNA-Trp after import into the mitochondrion. Moreover, several mitochondrial ...
The methionyl-tRNA synthetase (MetG) (EC:6.1.1.10) is a class I amino acyl-tRNA ligase. This family describes a region of the ... The aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of an amino acid to its cognate ... The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a ... In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2-hydroxyl of the tRNA ...
tRNA-charging. Amino acyl-tRNA Synthetases carry out a two-step reaction involving ATP.. ...
Phenylalanine-tRNA Ligase information including symptoms, causes, diseases, symptoms, treatments, and other medical and health ... Phenylalanyl T RNA Synthetase Source - MeSH 2007 Broader terms for Phenylalanine-tRNA Ligase. *Amino Acyl-tRNA Synthetases ... TRNA *Ligase Terms associated with Phenylalanine-tRNA Ligase:. Terms Similar to Phenylalanine-tRNA Ligase:. * ... Introduction: Phenylalanine-tRNA Ligase. Description of Phenylalanine-tRNA Ligase. Phenylalanine-tRNA Ligase: An enzyme that ...
  • Both the conventional AAtRS and their closely related paralogs often provide aminoacylated tRNAs for peptide ligations by MprF/Fem/MurM-type acetyltransferase fold ligases in the synthesis of peptidoglycan, N-end rule modifications of proteins, lipid aminoacylation or biosynthesis of antibiotics, such as valinamycin. (biomedcentral.com)
  • Alternatively they might supply aminoacylated tRNAs for other biosynthetic pathways like that for tetrapyrrole or directly function as peptide ligases as in the case of mycothiol and those identified here. (biomedcentral.com)
  • 10. The method of claim 1 wherein the tRNA molecule is aminoacylated by chemical misaminoacylation. (google.ca)
  • It aminoacylates at the 2'-OH of a terminal adenosine nucleotide on tRNA, and it is usually monomeric or dimeric (one or two subunits, respectively). (wikipedia.org)
  • It aminoacylates at the 3'-OH of a terminal adenosine on tRNA, and is usually dimeric or tetrameric (two or four subunits, respectively). (wikipedia.org)
  • McC is a heptapeptide with a formylated N-terminal methionine and a C-terminal aspartate whose α-carboxyl group is covalently linked to adenosine through an N -acyl phosphoramide bond ( 10 , 14 ). (asm.org)
  • Now that we know how AN2690 works, the same approach could be adapted to target other aminoacyl-tRNA synthetases with editing sites, which are also excellent targets for anti-microbial drugs," said Cusack, whose group performed the X-ray crystallography which revealed how AN2690 binds to LeuRS. (thefreedictionary.com)
  • Trbp111 selectively binds a noncovalently assembled tRNA-like structure. (ebi.ac.uk)
  • M. barkeri encodes a special amber suppressor tRNA (tRNA(Pyl)) that presumably recognizes this UAG codon. (nih.gov)
  • The identified mutation spectrum suggests that only mutation types that allow some residual tRNA-charging activity can result in the described mtARS diseases but the molecular mechanisms behind the selective tissue involvement are not currently understood. (nih.gov)
  • Pyrrolysyl-tRNA(Pyl) formation was presumed to result from subsequent modification of lysine attached to tRNA(Pyl). (nih.gov)
  • lysine and tRNA(Lys) are not substrates of the enzyme. (nih.gov)
  • In contrast, the LysRS1:LysRS2 complex does not recognize pyrrolysine and charges tRNA(Pyl) with lysine. (nih.gov)
  • Uruha A, Suzuki S, Suzuki N, Nishino I (2016) Perifascicular necrosis in anti-synthetase syndrome beyond anti-Jo 1. (springer.com)
  • After transfer to a nitrocellulose membrane, the samples were hybridized with a tRNA Pyl -specific oligonucleotide probe. (nih.gov)
  • To investigate whether pyrrolysine can be directly attached to tRNA(Pyl) we chemically synthesized pyrrolysine. (nih.gov)