A transfer RNA which is specific for carrying histidine to sites on the ribosomes in preparation for protein synthesis.
An essential amino acid that is required for the production of HISTAMINE.
An enzyme that catalyzes the conversion of linear RNA to a circular form by the transfer of the 5'-phosphate to the 3'-hydroxyl terminus. It also catalyzes the covalent joining of two polyribonucleotides in phosphodiester linkage. EC 6.5.1.3.
A guanine nucleotide containing one phosphate group esterified to the sugar moiety and found widely in nature.
An enzyme that is found in mitochondria and in the soluble cytoplasm of cells. It catalyzes reversible reactions of a nucleoside triphosphate, e.g., ATP, with a nucleoside diphosphate, e.g., UDP, to form ADP and UTP. Many nucleoside diphosphates can act as acceptor, while many ribo- and deoxyribonucleoside triphosphates can act as donor. EC 2.7.4.6.
Catalyze the joining of preformed ribonucleotides or deoxyribonucleotides in phosphodiester linkage during genetic processes. EC 6.5.1.
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.
A group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. EC 3.1.3.
An enzyme that catalyzes the transfer of a phosphate group to the 5'-terminal hydroxyl groups of DNA and RNA. EC 2.7.1.78.
A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.
The ultimate exclusion of nonsense sequences or intervening sequences (introns) before the final RNA transcript is sent to the cytoplasm.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A large superfamily of transcription factors that contain a region rich in BASIC AMINO ACID residues followed by a LEUCINE ZIPPER domain.
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.
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.
Enzymes that catalyze the S-adenosyl-L-methionine-dependent methylation of ribonucleotide bases within a transfer RNA molecule. EC 2.1.1.
An enzyme that catalyzes the decarboxylation of histidine to histamine and carbon dioxide. It requires pyridoxal phosphate in animal tissues, but not in microorganisms. EC 4.1.1.22.
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.
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.
A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.
The sequential set of three nucleotides in TRANSFER RNA that interacts with its complement in MESSENGER RNA, the CODON, during translation in the ribosome.
Poly(deoxyribonucleotide):poly(deoxyribonucleotide)ligases. Enzymes that catalyze the joining of preformed deoxyribonucleotides in phosphodiester linkage during genetic processes during repair of a single-stranded break in duplex DNA. The class includes both EC 6.5.1.1 (ATP) and EC 6.5.1.2 (NAD).
Preservative for wines, soft drinks, and fruit juices and a gentle esterifying agent.
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.
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.
An enzyme that catalyzes the first step of histidine catabolism, forming UROCANIC ACID and AMMONIA from HISTIDINE. Deficiency of this enzyme is associated with elevated levels of serum histidine and is called histidinemia (AMINO ACID METABOLISM, INBORN ERRORS).
A transfer RNA which is specific for carrying serine to sites on the ribosomes in preparation for protein synthesis.
The act of ligating UBIQUITINS to PROTEINS to form ubiquitin-protein ligase complexes to label proteins for transport to the PROTEASOME ENDOPEPTIDASE COMPLEX where proteolysis occurs.
A transfer RNA which is specific for carrying phenylalanine to sites on the ribosomes in preparation for protein synthesis.
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.
Complexes of enzymes that catalyze the covalent attachment of UBIQUITIN to other proteins by forming a peptide bond between the C-terminal GLYCINE of UBIQUITIN and the alpha-amino groups of LYSINE residues in the protein. The complexes play an important role in mediating the selective-degradation of short-lived and abnormal proteins. The complex of enzymes can be broken down into three components that involve activation of ubiquitin (UBIQUITIN-ACTIVATING ENZYMES), conjugation of ubiquitin to the ligase complex (UBIQUITIN-CONJUGATING ENZYMES), and ligation of ubiquitin to the substrate protein (UBIQUITIN-PROTEIN LIGASES).
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A transfer RNA which is specific for carrying tryptophan to sites on the ribosomes in preparation for protein synthesis.
A family of structurally related proteins that were originally discovered for their role in cell-cycle regulation in CAENORHABDITIS ELEGANS. They play important roles in regulation of the CELL CYCLE and as components of UBIQUITIN-PROTEIN 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.
A transfer RNA which is specific for carrying arginine to sites on the ribosomes in preparation for protein synthesis.
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).
A transfer RNA which is specific for carrying alanine to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying glycine to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying isoleucine to sites on the ribosomes in preparation for protein synthesis.
A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.
The rate dynamics in chemical or physical systems.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
One of the enzymes active in the gamma-glutamyl cycle. It catalyzes the synthesis of gamma-glutamylcysteine from glutamate and cysteine in the presence of ATP with the formation of ADP and orthophosphate. EC 6.3.2.2.
A transfer RNA which is specific for carrying glutamic acid to sites on the ribosomes in preparation for protein synthesis.
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.
A transfer RNA which is specific for carrying aspartic acid to sites on the ribosomes in preparation for protein synthesis.
A transfer RNA which is specific for carrying valine to sites on the ribosomes in preparation for protein synthesis.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
A transfer RNA which is specific for carrying glutamine to sites on the ribosomes in preparation for protein synthesis.
Ribonucleic acid in bacteria having regulatory and catalytic roles as well as involvement in protein synthesis.
A transfer RNA which is specific for carrying proline to sites on the ribosomes in preparation for protein synthesis.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Proteins found in any species of bacterium.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
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.
A DNA amplification technique based upon the ligation of OLIGONUCLEOTIDE PROBES. The probes are designed to exactly match two adjacent sequences of a specific target DNA. The chain reaction is repeated in three steps in the presence of excess probe: (1) heat denaturation of double-stranded DNA, (2) annealing of probes to target DNA, and (3) joining of the probes by thermostable DNA ligase. After the reaction is repeated for 20-30 cycles the production of ligated probe is measured.
A subset of ubiquitin protein ligases that are formed by the association of a SKP DOMAIN PROTEIN, a CULLIN DOMAIN PROTEIN and a F-BOX DOMAIN PROTEIN.
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).
A family of proteins that share the F-BOX MOTIF and are involved in protein-protein interactions. They play an important role in process of protein ubiquition by associating with a variety of substrates and then associating into SCF UBIQUITIN LIGASE complexes. They are held in the ubiquitin-ligase complex via binding to SKP DOMAIN PROTEINS.
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.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
The 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).
A transfer RNA which is specific for carrying threonine to sites on the ribosomes in preparation for protein synthesis.
A class of enzymes that form a thioester bond to UBIQUITIN with the assistance of UBIQUITIN-ACTIVATING ENZYMES. They transfer ubiquitin to the LYSINE of a substrate protein with the assistance of UBIQUITIN-PROTEIN LIGASES.
The penultimate step in the pathway of histidine biosynthesis. Oxidation of the alcohol group on the side chain gives the acid group forming histidine. Histidinol has also been used as an inhibitor of protein synthesis.
A reaction that introduces an aminoacyl group to a molecule. TRANSFER RNA AMINOACYLATION is the first step in GENETIC TRANSLATION.
An enzyme that activates serine with its specific transfer RNA. EC 6.1.1.11.
Ribonucleic acid in fungi having regulatory and catalytic roles as well as involvement in protein synthesis.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A zinc-binding domain defined by the sequence Cysteine-X2-Cysteine-X(9-39)-Cysteine-X(l-3)-His-X(2-3)-Cysteine-X2-Cysteine -X(4-48)-Cysteine-X2-Cysteine, where X is any amino acid. The RING finger motif binds two atoms of zinc, with each zinc atom ligated tetrahedrally by either four cysteines or three cysteines and a histidine. The motif also forms into a unitary structure with a central cross-brace region and is found in many proteins that are involved in protein-protein interactions. The acronym RING stands for Really Interesting New Gene.
An enzyme that activates histidine with its specific transfer RNA. EC 6.1.1.21.
A photoactivable URIDINE analog that is used as an affinity label.
A transfer RNA which is specific for carrying cysteine to sites on the ribosomes in preparation for protein synthesis.
An enzyme that catalyzes the first step of the pathway for histidine biosynthesis in Salmonella typhimurium. ATP reacts reversibly with 5-phosphoribosyl-1-pyrophosphate to yield N-1-(5'-phosphoribosyl)-ATP and pyrophosphate. EC 2.4.2.17.
The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.
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).
An enzyme that catalyzes the conversion of 4,5-dihydro-4-oxo-5-imidazolepropanoate to urocanate and water. EC 4.2.1.49.
Proteins prepared by recombinant DNA technology.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
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.
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.
Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.
A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme.
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.-.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
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 ... which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with ... "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-8. doi:10.1038/ ...
The fluorinated analog is incorporated into peptides via the relaxed substrate specificity of histidine-tRNA ligase and lowers ... Therefore, if a number of histidines are added to the end of the protein by genetic engineering, the affinity of the protein ... A polyhistidine-tag is an amino acid motif in proteins that typically consists of at least six histidine (His) residues, often ... When a compound having a structure similar to the histidine residue is added at a high concentration, the protein competes with ...
The eukaryotic homologs of RtcB, including the human RTCB protein, participates in the tRNA-splicing ligase complex. GRCh38: ... "Structures of the noncanonical RNA ligase RtcB reveal the mechanism of histidine guanylylation". Biochemistry. 52 (15): 2518-25 ... named after the eponymous protein in E. coli. The bacterial RtcB acts as a tRNA ligase, rejoining broken stem-loops in case of ... RNA 2',3'-cyclic phosphate and 5'-OH ligase is a protein that in humans is encoded by the RTCB gene. It is found in the stress ...
... glutamate-trna ligase MeSH D08.811.464.263.200.350 - glycine-trna ligase MeSH D08.811.464.263.200.400 - histidine-trna ligase ... proto-oncogene proteins c-mdm2 MeSH D08.811.464.938.750.750 - skp cullin f-box protein ligases MeSH D08.811.464.938.750.750.500 ... alanine-tRNA ligase MeSH D08.811.464.263.200.100 - arginine-tRNA ligase MeSH D08.811.464.263.200.150 - aspartate-tRNA ligase ... isoleucine-trna ligase MeSH D08.811.464.263.200.500 - leucine-trna ligase MeSH D08.811.464.263.200.550 - lysine-trna ligase ...
... glutamine-tRNA ligase EC 6.1.1.19: arginine-tRNA ligase EC 6.1.1.20: phenylalanine-tRNA ligase EC 6.1.1.21: histidine-tRNA ... butirosin acyl-carrier protein)-L-glutamate ligase EC 6.3.1.1: aspartate-ammonia ligase EC 6.3.1.2: glutamate-ammonia ligase EC ... threonine-tRNA ligase EC 6.1.1.4: leucine-tRNA ligase EC 6.1.1.5: isoleucine-tRNA ligase EC 6.1.1.6: lysine-tRNA ligase EC 6.1. ... valine-tRNA ligase EC 6.1.1.10: methionine-tRNA ligase EC 6.1.1.11: serine-tRNA ligase EC 6.1.1.12: aspartate-tRNA ligase EC ...
... such as the p38 subunit of aminoacyl-tRNA synthetase complex and far upstream element-binding protein 1 through addition of ... Ub transfer is aided by neighbouring residues histidine His433, which accepts a proton from Cys431 to activate it, and ... The precise function of this protein is unknown; however, the protein is a component of a multiprotein E3 ubiquitin ligase ... Suzuki H (September 2006). "Protein-protein interactions in the mammalian brain". The Journal of Physiology. 575 (Pt 2): 373-7 ...
B Leucine Leukotriene Ligase Lignin Limonene Linalool Linoleic acid Linolenic acid Lipase Lipid Lipid anchored protein ... tRNA) Triacsin C Thyroid-stimulating hormone (TSH) Thyrotropin-releasing hormone (TRH) Thyroxine (T4) Tocopherol (Vitamin E) ... HDL Histamine Histidine Histone Histone methyltransferase HLA antigen Homocysteine Hormone human chorionic gonadotropin (hCG) ... Granzyme Green fluorescent protein Growth factor Growth hormone Growth hormone-releasing hormone (GHRH) GTPase Guanine ...
... acyl-carrier-protein) dehydratase EC 4.2.1.60: now EC 4.2.1.59 EC 4.2.1.61: now EC 4.2.1.59 EC 4.2.1.62: 5a-hydroxysteroid ... histidine ammonia-lyase EC 4.3.1.4: formiminotetrahydrofolate cyclodeaminase EC 4.3.1.5: Now divided into EC 4.3.1.23 (tyrosine ... TRNA-intron endonuclease EC 4.99.1.1: ferrochelatase EC 4.99.1.2: alkylmercury lyase EC 4.99.1.3: sirohydrochlorin ... heme ligase "Enzyme: 4.1.2.8". Kyoto Encyclopedia of Genes and Genomes. Retrieved 2017-04-07. European Bioinformatics Institute ...
... encoding protein Hematopoietic cell signal transducer HRC: encoding protein Sarcoplasmic reticulum histidine-rich calcium- ... encoding enzyme Long-chain-fatty-acid-CoA ligase ANKRD24: encoding protein Ankyrin repeat domain-containing protein 24 ARMC6: ... Gene map locus 19q13.2 FCGBP: Fc fragment of IgG binding protein SARS2: seryl-tRNA synthetase 2, mitochondrial. Gene map locus ... encoding protein Zinc finger protein 112 ZNF134: encoding protein Zinc finger protein 134 ZNF160: encoding protein Zinc finger ...
"Protein Sci. 14 (12): 3039-47. doi:10.1110/ps.051604805. PMC 2253247. PMID 16322581.. ... Enzymes: CO CS and CN ligases (EC 6.1-6.3). 6.1: Carbon-Oxygen. *Aminoacyl tRNA synthetase *Alanine ... Stage two involves four key Mur ubiquitin ligase enzymes: MurC (EC),[1] MurD (EC),[2] MurE (EC) [3] and MurF (EC).[4] These ... 6-diaminopimelate ligase (MurE), and UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF). This entry also includes ...
Enzymes: CO CS and CN ligases (EC 6.1-6.3). 6.1: Carbon-Oxygen. *Aminoacyl tRNA synthetase *Alanine ... RCSB Protein Data Bank. Retrieved 2010-05-08.. *^ a b c d e Krajewski WW, Collins R, Holmberg-Schiavone L, Jones TA, Karlberg T ... histidine, carbamoyl phosphate, glucosamine-6-phosphate, cytidine triphosphate (CTP), and adenosine monophosphate (AMP).[5][8][ ... "Glutamine synthetase inactivation by protein-protein interaction". Proceedings of the National Academy of Sciences of the ...
Enzymes: CO CS and CN ligases (EC 6.1-6.3). 6.1: Carbon-Oxygen. *Aminoacyl tRNA synthetase *Alanine ... The small subunit has a 3-layer beta/beta/alpha structure, and is thought to be mobile in most proteins that carry it. The C- ... DNA sequence and evolution of the CPS domain of the Syrian hamster multifunctional protein CAD". J. Biol. Chem. 265 (18): 10395 ...
Membrane-associated ligases[edit]. Some ligases associate with biological membranes as peripheral membrane proteins or anchored ... Enzymes: CO CS and CN ligases (EC 6.1-6.3). 6.1: Carbon-Oxygen. *Aminoacyl tRNA synthetase *Alanine ... The common names of ligases often include the word "ligase", such as DNA ligase, an enzyme commonly used in molecular biology ... DNA ligase. References[edit]. *^ "Synthases and ligases". chem.qmul.ac.uk. Archived from the original on October 15, 2012. ...
An aminoacyl-tRNA synthetase (aaRS or ARS), also called tRNA-ligase, is an enzyme that attaches the appropriate amino acid onto ... Aminoacyl tRNA therefore plays an important role in RNA translation, the expression of genes to create proteins. ... If the incorrect tRNA is added (aka. the tRNA is found to be improperly charged), the aminoacyl-tRNA bond is hydrolyzed. This ... Delarue, M (1995). "Aminoacyl-tRNA synthetases". Structural Biology. 5: 48-55.. *^ "Molecule of the Month: Aminoacyl-tRNA ...
... that the RNase-P RNA subunit could catalyze the cleavage of precursor tRNA into active tRNA in the absence of any protein ... a protein that catalyzes the same reaction, uses a coordinating histidine and lysine to act as a base to attack the phosphate ... One approach for selecting a ligase ribozyme involves using biotin tags, which are covalently linked to the substrate. If a ... which is responsible for conversion of a precursor tRNA into the active tRNA. Much to their surprise, they found that RNase-P ...
protein binding. • enzyme binding. • metal ion binding. • identical protein binding. • ubiquitin protein ligase binding. • p53 ... Enzymes: CO CS and CN ligases (EC 6.1-6.3). 6.1: Carbon-Oxygen. *Aminoacyl tRNA synthetase *Alanine ... protein N-terminus binding. • ubiquitin protein ligase activity. • NEDD8 ligase activity. • disordered domain specific binding ... Mouse double minute 2 homolog (MDM2) also known as E3 ubiquitin-protein ligase Mdm2 is a protein that in humans is encoded by ...
... a ubiquitin ligase. The complex moves into the nucleus where Siah1 targets nuclear proteins for degradation, thus initiating ... tRNA, Hepatitis A viral RNA, Hepatitis B viral RNA, Hepatitis C viral RNA, HPIV3, lymphokine mRNA, IFN-γ mRNA, JEV mRNA, and ... The hemithioacetal is deprotonated by a histidine residue in the enzyme's active site (general base catalysis). Deprotonation ... Svedružić Ž.M.; Odorčić I.; Chang C.H.; Svedružić D. (2020). "Substrate Channeling via a Transient Protein-Protein Complex: The ...
Enzymes: CO CS and CN ligases (EC 6.1-6.3). 6.1: Carbon-Oxygen. *Aminoacyl tRNA synthetase *Alanine ... proteins. In enzymology, a phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) is an enzyme that catalyzes the chemical ... L-glutamine amido-ligase, (ADP-forming), 2-N-formyl-1-N-(5-phospho-D-ribosyl)glycinamide:L-glutamine, and amido-ligase (ADP- ... This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ...
... and the resulting gaps are replaced with DNA and joined via DNA ligase. A protein is a polymer that is composed from amino ... tRNA ↽ − − ⇀ aminoacyl − tRNA + AMP {\displaystyle {\ce {{Aminoacyl-AMP}+ tRNA <=> {aminoacyl-tRNA}+ AMP}}} The combination of ... threonine and tryptophan for adults and histidine, and arginine for babies are obtained through diet. The general structure of ... This reaction, called tRNA charging, is catalyzed by aminoacyl tRNA synthetase. A specific tRNA synthetase is responsible for ...
... mitogen-activated protein kinase kinase EC 2.7.13.1: protein-histidine pros-kinase EC 2.7.13.2: protein-histidine tele-kinase ... tRNA (cytosine-5-)-methyltransferase EC 2.1.1.30: deleted EC 2.1.1.31: tRNA (guanine-N1-)-methyltransferase EC 2.1.1.32: tRNA ( ... protein ligase EC 2.7.7.64: UTP-monosaccharide-1-phosphate uridylyltransferase EC 2.7.7.65: diguanylate cyclase EC 2.7.7.66: ... cAMP-dependent protein kinase EC 2.7.11.12: cGMP-dependent protein kinase EC 2.7.11.13: protein kinase C EC 2.7.11.14: ...
... acyl-carrier-protein) phosphodiesterase EC 3.1.4.15: adenylyl-(glutamate-ammonia ligase) hydrolase EC 3.1.4.16: 2',3'-cyclic- ... tRNA-intron endonuclease EC 3.1.27.10: rRNA endonuclease EC 3.1.30.1: Aspergillus nuclease S1 EC 3.1.30.2: Serratia marcescens ... aminoacyl-histidine dipeptidase, carnosinase, now EC 3.4.13.3 EC 3.4.3.4: aminoacyl-methylhistidine dipeptidase, anserinase, ... protein-secreting ATPase EC 3.6.3.51: mitochondrial protein-transporting ATPase EC 3.6.3.52: chloroplast protein-transporting ...
Enzymes: CO CS and CN ligases (EC 6.1-6.3). 6.1: Carbon-Oxygen. *Aminoacyl tRNA synthetase *Alanine ... proteins. Asparagine synthase (glutamine-hydrolysing) (EC 6.3.5.4, asparagine synthetase (glutamine-hydrolysing), glutamine- ... L-glutamine amido-ligase (AMP-forming).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction ...
transfer RNA (tRNA) - transfers specific amino acids to growing polypeptide chains at the ribosomal site of protein synthesis ... 2.7.13: protein-histidine. *Protein-histidine pros-kinase. *Protein-histidine tele-kinase ... Transfer RNA (tRNA)-transfers specific amino acids to growing polypeptide chains at the ribosomal site of protein synthesis ... RNA polymerase III synthesizes tRNAs, rRNA 5S and other small RNAs found in the nucleus and cytosol. RNA polymerase IV and V ...
These families have been documented in dozens of different protein and protein family databases such as Pfam. Enzymes are ... For instance, two ligases of the same EC number that catalyze exactly the same reaction can have completely different sequences ... Ibba M, Soll D (2000). "Aminoacyl-tRNA synthesis". Annual Review of Biochemistry. 69: 617-50. doi:10.1146/annurev.biochem.69.1. ... "Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase ...
protein homodimerization activity. • kynureninase activity. • catalytic activity. • pyridoxal phosphate binding. • hydrolase ... HISTIDINE→. *Histidine ammonia-lyase. *Urocanate hydratase. *Formiminotransferase cyclodeaminase. proline→. *Proline oxidase. * ...
2.7.13: protein-histidine. *Protein-histidine pros-kinase. *Protein-histidine tele-kinase ... A number of genuine CK structures have been solved by high-resolution electron microscopy and protein X-ray crystallography by ...
Human protein Protein description from UniProt Pfam family with Human protein 1. SdhA. SDHA_HUMAN. Succinate dehydrogenase [ ... The histidine residue decreases the pKa of tyrosine, making it more suitable to donate its proton to the reduced ubiquinone ... Historically, the SdhE protein was once considered a hypothetical protein.[9] YgfY was also thought to be involved in ... In molecular biology, the protein domain named Sdh5 is also named SdhE which stands for succinate dehydrogenase protein E. In ...
Pfam protein domain database. More...Pfami. View protein in Pfam. PF03129, HGTP_anticodon, 1 hit. PF13393, tRNA-synt_His, 1 ... IPR006195, aa-tRNA-synth_II. IPR004154, Anticodon-bd. IPR036621, Anticodon-bd_dom_sf. IPR015807, His-tRNA-ligase. IPR041715 ... MF_00127, His_tRNA_synth, 1 hit. InterProi. View protein in InterPro. IPR006195, aa-tRNA-synth_II. IPR004154, Anticodon-bd ... sp,Q028M4,SYH_SOLUE Histidine--tRNA ligase OS=Solibacter usitatus (strain Ellin6076) OX=234267 GN=hisS PE=3 SV=1 ...
Pfam protein domain database. More...Pfami. View protein in Pfam. PF03129 HGTP_anticodon, 1 hit. PF13393 tRNA-synt_His, 1 hit ... View protein in InterPro. IPR006195 aa-tRNA-synth_II. IPR004154 Anticodon-bd. IPR036621 Anticodon-bd_dom_sf. IPR015807 His-tRNA ... View protein in InterPro. IPR006195 aa-tRNA-synth_II. IPR004154 Anticodon-bd. IPR036621 Anticodon-bd_dom_sf. IPR015807 His-tRNA ... sp,Q1BGX3,SYH_BURCA Histidine--tRNA ligase OS=Burkholderia cenocepacia (strain AU 1054) OX=331271 GN=hisS PE=3 SV=1 ...
... are ubiquitously expressed enzymes responsible for ligating amino acids to cognate tRNA molecules. Mutations in four genes ... Green Fluorescent Proteins / genetics * Green Fluorescent Proteins / metabolism * Histidine-tRNA Ligase / genetics* ... Aminoacyl-tRNA synthetases (ARSs) are ubiquitously expressed enzymes responsible for ligating amino acids to cognate tRNA ... A loss-of-function variant in the human histidyl-tRNA synthetase (HARS) gene is neurotoxic in vivo Hum Mutat. 2013 Jan;34(1): ...
The Histidyl-tRNA Synthetase is fused to 6xHis Tag and purified by proprietary chromatographic techniques. ... Recombinant Human Histidyl-tRNA Synthetase produced inbaculovirusis a single, glycosylated, polypeptide chain having a ... histidine-tRNA ligase activity; histidine-tRNA ligase activity; nucleotide binding. Products Types ◆ Recombinant Protein HARS- ... HARS; histidyl-tRNA synthetase; HRS; FLJ20491; histidine tRNA ligase 1, cytoplasmic; EC 6.1.1.21; HisRS; histidine-tRNA ligase ...
histidine-tRNA ligase activity. protein binding. ATP binding. protein homodimerization activity. poly(A) RNA binding. ... histidine tRNA ligase 2, mitochondrial (putative); Histidine--tRNA ligase-like; histidine-tRNA ligase homolog; Histidyl-tRNA ... Probable histidine--tRNA ligase, mitochondrial; probable histidyl-tRNA synthetase, mitochondrial; Probable histidyl-tRNA ... Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this ...
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 ... which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with ... "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-8. doi:10.1038/ ...
... also known as histidine-tRNA ligase, is an enzyme which in humans is encoded by the HARS gene. The protein encoded by this gene ... Histidyl-tRNA synthetase and asparaginyl-tRNA synthetase, autoantigens in myositis, activate chemokine receptors on T ... Autoantibodies to histidyl t-RNA synthetase, termed as anti-Jo-1, or to other amino acyl t-RNA synthetase occur in 25% of ... histidyl t-RNA synthetase. Histidyl-tRNA synthetase (HARS) ... Hatakeyama S, TRIM proteins and cancer. Nat Rev Cancer 2011; 11 ...
Protein Coding), Histidyl-TRNA Synthetase 2, Mitochondrial, including: function, proteins, disorders, pathways, orthologs, and ... Protein Symbol:. P49590-SYHM_HUMAN. Recommended name:. Histidine--tRNA ligase, mitochondrial. Protein Accession:. P49590. ... Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this ... Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this ...
Protein Coding), Histidyl-TRNA Synthetase 1, including: function, proteins, disorders, pathways, orthologs, and expression. ... Protein Symbol:. P12081-SYHC_HUMAN. Recommended name:. Histidine--tRNA ligase, cytoplasmic. Protein Accession:. P12081. ... Cytoplasmic histidine--tRNA ligase (Probable). Plays a role in axon guidance. *SYHC_HUMAN,P12081 ... Cytoplasmic histidine--tRNA ligase (Probable). Plays a role in axon guidance. *SYHC_HUMAN,P12081 ...
cceu:CBR64_18065 histidine--tRNA ligase K01892 464 117 ( -) 33 0.304 204 -, 1 dai:Desaci_4455 UDP-glucose pyrophosphorylase ... 18433344 E4 SUMO-protein ligase PIAL2 isoform X1 K04706 1024 102 ( 1) 29 0.309 97 ,-, 3 azc:AZC_1424 nitrite extrusion protein ... deu:DBW_1931 phenylacetate--coenzyme A ligase K01912 435 100 ( -) 29 0.333 78 -, 1 dgo:DGo_CA0403 MoeA-like protein, domain I ... tbe:Trebr_0253 tRNA modification GTPase mnmE K03650 509 100 ( -) 29 0.310 113 ,-, 1 tdn:Suden_1637 GTP-binding protein LepA ...
Histidine-trna Ligase. An enzyme that activates histidine with its specific transfer RNA. EC 6.1.1.21. ... Histidine Kinase. A member of the transferase superfamily of proteins. In the activated state, protein-histidine kinase ... Histidine Therapy: A Project to Treat HARS Deficiency. This study evaluates the role of histidine in patients with HARS ... Histidine Ammonia-lyase. An enzyme that catalyzes the first step of histidine catabolism, forming UROCANIC ACID and AMMONIA ...
... catalyze aminoacylation of tRNAs in the cytoplasm. Surprisingly, AARSs also have critical extracellular and nuclear functions. ... Protein Isoforms * Histidine-tRNA Ligase Associated data * PDB/4G84 * PDB/4G85 Grant support * GM 23562/GM/NIGMS NIH HHS/United ... Using disease-associated histidyl-tRNA synthetase (HisRS) as an example, we found an expressed 171-amino acid protein (HisRSΔCD ... Aminoacyl-tRNA synthetases (AARSs) catalyze aminoacylation of tRNAs in the cytoplasm. Surprisingly, AARSs also have critical ...
Histidyl tRNA synthetase HisRSHistidine tRNA ligase Uniprot ID: Q2KI84mRNA RefSeq: NM_001046066Protein RefSeq: NP_001039531 ... Histidyl tRNA synthetase. HisRS. Histidine tRNA ligase. Uniprot ID: Q2KI84. mRNA RefSeq: NM_001046066. Protein RefSeq: NP_ ... The existence of autoantibodies to nuclear and cytoplasmic antigens, in particular to the aminoacyl-tRNA synthetase group of ... and can immunoprecipitate labelled enzyme as well as its specific tRNA. HRS has a molecular weight of 55 kDa in SDS- ...
Cusabios recombinant protein are validated under strict QC standards to ensure the performance. If the product does not ... Recombinant Histidine--tRNA ligase(hisS). CSB-YP341635MVN. CSB-EP341635MVN. CSB-BP341635MVN. CSB-MP341635MVN. Yeast. E.coli. ... Recombinant Lysine--tRNA ligase(lysS) ,partial. CSB-YP341648MVN. CSB-EP341648MVN. CSB-BP341648MVN. CSB-MP341648MVN. Yeast. E. ... Recombinant Tryptophan--tRNA ligase, mitochondrial(wars-2) ,partial. CSB-YP341629CXY. CSB-EP341629CXY. CSB-BP341629CXY. CSB- ...
This array format can be utilized for screening protein-protein interact ... Protein Arrays are a versatile and innovative series of products featuring recombinant or purified proteins spotted in ... Glycine-tRNA ligase. * Histidine-tRNA ligase. * Histone H2A. * Histone H2B. * LC-1. ... Protein Arrays RayBio® Protein Arrays are a versatile and innovative series of products featuring immobilized proteins spotted ...
Histidine--tRNA ligase; Histidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation ... Histidine--tRNA ligase; Histidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation ... Histidine--tRNA ligase; Histidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation ... Histidine--tRNA ligase; Histidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation ...
We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their ... InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites ... The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, lysine, phenylalanine, proline, serine, ... Isoleucine-tRNA ligase (IPR002301). Short name: Ile-tRNA-ligase Family relationships *Isoleucine-tRNA ligase (IPR002301) * ...
We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their ... InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites ... The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, lysine, phenylalanine, proline, serine, ... Glu-tRNA-ligase_bac/mito Family relationships *Glutamyl/glutaminyl-tRNA synthetase (IPR000924) *Glutamate-tRNA ligase, ...
We have developed a second orthogonal tRNA/synthetase pair for use in yeast based on the Escherichia coli tRNALeu/leucyl tRNA- ... Histidine / genetics, metabolism. Humans. Leucine-tRNA Ligase / genetics*, metabolism*. Methyltyrosines / genetics, metabolism* ... 0/Methyltyrosines; 0/Octanoic Acids; 0/Proteins; 0/RNA, Transfer, Amino Acyl; 3308-72-3/O-methyltyrosine; 52-90-4/Cysteine; 71- ... 00-1/Histidine; EC 1.15.1.1/Superoxide Dismutase; EC 6.1.1.4/Leucine-tRNA Ligase ...
... full-length cDNA coding fused to ahexa-histidine purification tag. Expressed by recombinant baculovirus(Autographa californica ... histidine tRNA ligase 1; cytoplasmic; EC 6.1.1.21; FLJ20491; HisRS; histidine translase; Histidine tRNA ligase; Histidyl tRNA ... Human Histidyl-TRNA Synthetase [His] (DAG603) Human Histidyl-TRNA Synthetase [His], recombinant protein from Baculovirus ... Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this ...
We offer monoclonal and polyclonal antibodies as well as purified recombinant proteins and antigens for research. Learn more ... FLJ20491, HRS, HisRS, Histidine--tRNA ligase, Histidyl-tRNA synthetase, cytoplasmic. Species. Human. ... which is essential for the incorporation of histidine into proteins. HARS is a frequent target of autoantibodies in the human ... HARS, also known as Histidyl-tRNA synthetase, function to catalyze the aminoacylation of tRNAs by their corresponding amino ...
Histidine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology ... Histidine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology ... Histidine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology ... Histidine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology ...
Sood, R. ; Wek, R. C. / GCN2, an eIF-2a protein kinase containing sequences related to aminoacyl-trna synthetases, is conserved ... Sood, R., & Wek, R. C. (1997). GCN2, an eIF-2a protein kinase containing sequences related to aminoacyl-trna synthetases, is ... Sood, R & Wek, RC 1997, GCN2, an eIF-2a protein kinase containing sequences related to aminoacyl-trna synthetases, is ... GCN2, an eIF-2a protein kinase containing sequences related to aminoacyl-trna synthetases, is conserved from yeast to mammals. ...
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this ... Functioning in the synthesis of histidyl-transfer RNA, the enzyme plays an accessory role in the regulation of protein ... gene is an enzyme belonging to the class II family of aminoacyl-tRNA synthetases. ...
Genetic information processingProtein synthesistRNA aminoacylationhistidine--tRNA ligase (TIGR00442; EC 6.1.1.21; HMM-score: ... Protein synthesis (provided by Aureolib)[edit source , edit]. *Aureolib: no data available ... no clan definedHPS6; Hermansky-Pudlak syndrome 6 protein (PF15702; HMM-score: 13) ...
... generated by lysine tRNA ligase, as well as Met-AMP, His-AMP and Asp-AMP, lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine ... Modulates proteasomal degradation of target proteins by the SCF (SKP2-CUL1-F-box protein) E3 ubiquitin-protein ligase complex. ... Protein kinase C-interacting protein 1. Gene Name. HINT1. Organism. Humans. Amino acid sequence. ,lcl,BSEQ0016443,Histidine ... Histidine triad nucleotide-binding protein 1 up-regulates cellular levels of p27KIP1 by targeting ScfSKP2 ubiquitin ligase and ...
Histidyl-tRNA synthetase; EC=6.1.1.21;AltName: Full=Histidine--tRNA ligase; Short=HisRS; Homologs Archaea 66/68 : Bacteria 868/ ... tRNA aminoacylation for protein translation,PF00587,IPR002314, GO:PFM GO:0004812,GO:aminoacyl-tRNA ligase activity,PF03129, ... Histidyl-tRNA synthetase; EC=6.1.1.21;AltName: Full=Histidine--tRNA ligase; Short=HisRS; SW:GN Name=hisS; OrderedLocusNames= ... aminoacyl-tRNA ligase activity,Aminoacyl-tRNA synthetase, GO:SWS GO:0005524,GO:ATP binding,ATP-binding, GO:SWS GO:0005737, ...
The fluorinated analog is incorporated into peptides via the relaxed substrate specificity of histidine-tRNA ligase and lowers ... Therefore, if a number of histidines are added to the end of the protein by genetic engineering, the affinity of the protein ... A polyhistidine-tag is an amino acid motif in proteins that typically consists of at least six histidine (His) residues, often ... When a compound having a structure similar to the histidine residue is added at a high concentration, the protein competes with ...
Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..428 FT /note="Histidine--tRNA ligase" FT / ... DR GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; ... DE RecName: Full=Histidine--tRNA ligase {ECO:0000255,HAMAP-Rule:MF_00127}; DE EC=6.1.1.21 {ECO:0000255,HAMAP-Rule:MF_00127}; DE ... TRNA_LIGASE_II; 1. PE 3: Inferred from homology; DR PRODOM; Q0IDK4. DR SWISS-2DPAGE; Q0IDK4. KW Aminoacyl-tRNA synthetase; ATP- ...
Interconnected RNA processing mechanisms ensure the fidelity of non-conventional mRNA splicing during the unfolded protein ... 1996) tRNA ligase is required for regulated mRNA splicing in the unfolded protein response Cell 87:405-413. ... This conserved histidine (His182 in ctTrl1) is surface-exposed and located on the periphery of the active-site groove in the ... Full-length ctTrl1 (NCBI Entrez Gene ID: 18257519, CTHT_0034810 tRNA ligase-like protein) was cloned from C. thermophilum cDNA ...
  • Here, we present results from a mutation screen of the histidyl-tRNA synthetase (HARS) gene in a large cohort of patients with peripheral neuropathy. (nih.gov)
  • Recombinant Human Histidyl-tRNA Synthetase produced in baculovirus is a single, glycosylated, polypeptide chain having a molecular mass of 58.3 kDa. (creativebiomart.net)
  • The Histidyl-tRNA Synthetase is fused to 6xHis Tag and purified by proprietary chromatographic techniques. (creativebiomart.net)
  • Strongly reactive with human anti Histidyl-tRNA Synthetase antisera. (creativebiomart.net)
  • Lyophilized Histidyl-tRNA Synthetase although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles. (creativebiomart.net)
  • Histidyl-tRNA synthetase (HARS) also known as histidine-tRNA ligase, is an enzyme which in humans is encoded by the HARS gene. (wikipedia.org)
  • HARS2 (Histidyl-TRNA Synthetase 2, Mitochondrial) is a Protein Coding gene. (genecards.org)
  • Mitochondrial aminoacyl-tRNA synthetase that catalyzes the ATP-dependent ligation of histidine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (His-AMP). (genecards.org)
  • HARS1 (Histidyl-TRNA Synthetase 1) is a Protein Coding gene. (genecards.org)
  • Using disease-associated histidyl-tRNA synthetase (HisRS) as an example, we found an expressed 171-amino acid protein (HisRSΔCD) that deleted the entire CD, and joined an N-terminal WHEP to the C-terminal anticodon-binding domain (ABD). (nih.gov)
  • The existence of autoantibodies to nuclear and cytoplasmic antigens, in particular to the aminoacyl-tRNA synthetase group of enzymes, in the sera of up to 89% of patients indicates that these diseases have an autoimmune origin. (afsbio.com)
  • Isoleucine-tRNA ligase (also known as Isoleucyl-tRNA synthetase)( EC:6.1.1.5 ) is an alpha monomer that belongs to class Ia. (ebi.ac.uk)
  • The aminoacyl-tRNA synthetase (also known as aminoacyl-tRNA ligase) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction [ PMID: 10704480 , PMID: 12458790 ]. (ebi.ac.uk)
  • Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin. (ebi.ac.uk)
  • The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules. (ebi.ac.uk)
  • Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase. (ebi.ac.uk)
  • The aminoacyl-tRNA synthetase family: modules at work. (ebi.ac.uk)
  • Recombinanthuman histidyl-tRNA synthetase (Jo-1) full-length cDNA coding fused to ahexa-histidine purification tag. (creative-diagnostics.com)
  • We have developed a second orthogonal tRNA/synthetase pair for use in yeast based on the Escherichia coli tRNALeu/leucyl tRNA-synthetase pair. (biomedsearch.com)
  • Using a novel genetic selection, we have identified a series of synthetase mutants that selectively charge the amber suppresor tRNA with the C8 amino acid, alpha-aminocaprylic acid, and the photocaged amino acid, o-nitrobenzyl cysteine, allowing them to be inserted into proteins in yeast in response to the amber nonsense codon, TAG. (biomedsearch.com)
  • HARS, also known as Histidyl-tRNA synthetase, function to catalyze the aminoacylation of tRNAs by their corresponding amino acids. (arp1.com)
  • Uncharged tRNA that accumulates during amino acid starvation is thought to bind to the synthetase-related domain and stimulate GCN2 phosphorylation of eIF-2n. (elsevier.com)
  • Chou TF, Tikh IB, Horta BA, Ghosh B, De Alencastro RB, Wagner CR: Engineered monomeric human histidine triad nucleotide-binding protein 1 hydrolyzes fluorogenic acyl-adenylate and lysyl-tRNA synthetase-generated lysyl-adenylate. (drugbank.ca)
  • SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. (univ-lyon1.fr)
  • The HARS2 gene provides instructions for making an enzyme called mitochondrial histidyl-tRNA synthetase. (medlineplus.gov)
  • Enzymes called aminoacyl-tRNA synthetases, including mitochondrial histidyl-tRNA synthetase, attach a particular amino acid to a specific tRNA. (medlineplus.gov)
  • Mitochondrial histidyl-tRNA synthetase attaches the amino acid histidine to the correct tRNA, which helps ensure that histidine is added at the proper place in the mitochondrial protein. (medlineplus.gov)
  • The HARS2 gene mutations involved in Perrault syndrome reduce the activity of mitochondrial histidyl-tRNA synthetase. (medlineplus.gov)
  • A shortage of functional mitochondrial histidyl-tRNA synthetase prevents the normal assembly of new proteins within mitochondria. (medlineplus.gov)
  • Mutations in mitochondrial histidyl tRNA synthetase HARS2 cause ovarian dysgenesis and sensorineural hearing loss of Perrault syndrome. (medlineplus.gov)
  • Zusätzlich bieten wir Ihnen Histidyl TRNA Synthetase Antikörper (76) und Histidyl TRNA Synthetase Proteine (15) und viele weitere Produktgruppen zu diesem Protein an. (antikoerper-online.de)
  • Secreted histidyl-tRNA synthetase splice variants elaborate major epitopes for autoantibodies in inflammatory myositis. (antikoerper-online.de)
  • Findings suggest that histidyl-tRNA synthetase (HARS ) is associated with axonal peripheral neuropathy. (antikoerper-online.de)
  • Demonstrating histidyl-tRNA synthetase (Jo-1)-specific T cell responses represents a key step in establishing the hypothesis that Jo-1 drives T cell-mediated autoimmunity in Jo-1+ polymyositis. (antikoerper-online.de)
  • This all alpha helical domain is the anticodon binding domain of Arginyl tRNA synthetase. (embl.de)
  • This all alpha helical domain is the anticodon binding domain (ABD) of arginyl tRNA synthetase, and also matches the ABD of some glycine tRNA synthetases. (embl.de)
  • Aminoacyl-tRNA synthetase (aaRS) is a key enzyme during protein biosynthesis. (embl.de)
  • Although antigenic triggers for this process remain undefined, clinically homogeneous subsets of PM patients are characterized by autoantibodies directed against nuclear and cytoplasmic Ags that include histidyl-tRNA synthetase (Jo-1). (elsevier.com)
  • A major determinant for binding and aminoacylation of tRNA(Ala) in cytoplasmic Alanyl-tRNA synthetase is mutated in dominant axonal Charcot-Marie-Tooth disease. (expasy.org)
  • Activation reactions include formation of phosphates (peptidoglycan, glutathione) or of adenylates (aminoacyl-tRNA-ligases, gramicidin S-synthetase). (springer.com)
  • Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNA(Val) and valyl-tRNA synthetase. (syshospital.org)
  • GCN2 is a multidomain protein with a kinase region juxtaposed to sequences homologous to the histidyl-tRNA synthetases (HisRS). (elsevier.com)
  • This study suggests that the human HisRS genes, while descending from a common ancestor with dual function for both types of tRNA(His), have acquired highly specialized tRNA recognition properties through evolution. (antikoerper-online.de)
  • Data suggest that by comparing human and trypanosomatid histidyl-tRNA synthetases ( HisRS ) may provide opportunities for developing specific inhibitors of Trypanosoma brucei HisRS . (antikoerper-online.de)
  • The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. (creativebiomart.net)
  • The protein encoded by this gene is a cytoplasmic enzyme which belongsto the class II family of aminoacyl-tRNA synthetases. (creative-diagnostics.com)
  • It is believed that the N-terminal sensor domain of the cytoplasmic histidine kinase KinA is responsible for detection of the sporulation-specific signal(s) that appears to be produced only under starvation conditions. (usda.gov)
  • We found cytoplasmic proteins involved in glycolysis to be highly expressed in post-exponential phase while proteins involved in tricarboxylic acid cycle to be prevalent in stationary phase. (usf.edu)
  • These cytoplasmic proteins are members of the DIPP subfamily of Nudix hydrolases, and differ from each other by a single amino acid. (biomedcentral.com)
  • Among its related pathways are tRNA Aminoacylation and Gene Expression . (genecards.org)
  • Gene Ontology (GO) annotations related to this gene include aminoacyl-tRNA ligase activity . (genecards.org)
  • Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. (ebi.ac.uk)
  • The fungal tRNA ligase Trl1 (previously named Rlg1) is encoded by an essential gene and is involved in tRNA splicing and the unfolded protein response (UPR). (elifesciences.org)
  • Trithorax proteins, including the Arabidopsis Trithorax-like protein ATX1, are histone modifiers regulating gene activity. (usda.gov)
  • Thus, there are many examples where one analysis of a eukaryotic gene or protein has recovered the 3-domains tree, but a different analysis of the same molecule(s) has recovered the eocyte tree ( , 1 , , 8 - , 10 , , 13 - , 17 ). (pnas.org)
  • The core gene set includes the greatmajority of genes coding for proteins involved in genome replication andexpression, but only a relatively small subset of metabolic functions. (embl-heidelberg.de)
  • Gene expression is controlled by transcriptional regulatory proteins, which bind specific DNA sequences and recruit cofactors and the transcription apparatus to promoters ( 1 - 3 ). (sciencemag.org)
  • Peptide mass fingerprints, acquired by matrix-assisted laser desorption/ionisation-(MALDI) mass spectrometry, enabled unambiguous protein identifications to be made where full gene sequence information was available. (edu.au)
  • In some instances, several protein spots appeared to be encoded by the same gene, indicating that post-translational modification and/or alternative splicing events may be a common feature of functional gene expression in T. gondii. (edu.au)
  • Transcription regulation mechanism of the syntaxin 1A gene via protein kinase A Syntaxin 1A (Stx1a) is primarily involved in the docking of synaptic vesicles at active zones in neurons. (medworm.com)
  • In the present study, to clarify the factor characterizing Stx1a gene expression via the protein kinase A (PKA) pathway inducing the Stx1a mRNA, we investigated whether the epigenetic process is involved in the Stx1a gene transcription induced by PKA signaling. (medworm.com)
  • Functioning in the synthesis of histidyl-transfer RNA, the enzyme plays an accessory role in the regulation of protein biosynthesis. (genecards.org)
  • Required for the first step of histidine biosynthesis. (string-db.org)
  • Protein biosynthesis. (nig.ac.jp)
  • They play key roles in biosynthesis pathways of oligo- and polysaccharides, as well as protein glycosylation and formation of valuable natural products (Lairson et al. (springeropen.com)
  • Operons that embrace a complete complement of pathway-specific structural genes (whole-pathway operons), such as the ones encoding all the enzymes of tryptophan (Trp) biosynthesis or histidine biosynthesis, have a classical status in both biochemistry and molecular genetics that extends far beyond understanding these pathways per se. (asm.org)
  • Despite these regulatory differences the mechanisms of siderophore biosynthesis follow the same fundamental enzymatic logic, which involves a series of elongating acyl-S-enzyme intermediates on multimodular protein assembly lines: nonribosomal peptide synthetases (NRPS). (asm.org)
  • The third is the yeast kinase GCN2 which alters protein synthesis in response to amino acid starvation. (elsevier.com)
  • Sood, R & Wek, RC 1997, ' GCN2, an eIF-2a protein kinase containing sequences related to aminoacyl-trna synthetases, is conserved from yeast to mammals ', FASEB Journal , vol. 11, no. 9, pp. (elsevier.com)
  • Lima CD, Klein MG, Weinstein IB, Hendrickson WA: Three-dimensional structure of human protein kinase C interacting protein 1, a member of the HIT family of proteins. (drugbank.ca)
  • The ligase/adenylyltransferase domain (LIG) is shown in blue, the polynucleotide kinase domain (KIN) in white, the cyclic phosphodiesterase domain (CPD) in green. (elifesciences.org)
  • single download R-Smads( DSBs) in the kinase can act directed via a Similarly only MH2 inhibitor hCG( HRR) excision, or through same such complex reading( NHEJ), normal protein resulting( growth) and robust prostacyclin alleviating( MMEJ) receptors. (erik-mill.de)
  • The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. (creativebiomart.net)
  • Jo-1 autoantibodies are capable of inhibiting the activity of the target antigen (HRS) and can immunoprecipitate labelled enzyme as well as its specific tRNA. (afsbio.com)
  • The enzyme, isoleucine-tRNA ligase, activates not only the cognate substrate L-isoleucine but also the minimally distinct L-valine in the first, aminoacylation step. (ebi.ac.uk)
  • Yeast tRNA ligase (Trl1) is an essential trifunctional enzyme that catalyzes exon-exon ligation during tRNA biogenesis and the non-conventional splicing of HAC1 mRNA during the unfolded protein response (UPR). (elifesciences.org)
  • This enzyme is important in the production (synthesis) of proteins in cellular structures called mitochondria, the energy-producing centers in cells. (medlineplus.gov)
  • p>Sequence annotations describe regions or sites of interest in the protein sequence, such as post-translational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. (uniprot.org)
  • Furthermore, L-Histidine and beta-alanine can be converted into carnosine through the action of the enzyme carnosine synthase 1. (bovinedb.ca)
  • Finally, beta-Alanine and L-histidine can be biosynthesized from carnosine through the action of the enzyme Beta-ala-his dipeptidase. (bovinedb.ca)
  • To study the role of conformational changes within the protein catalyst and the DNA substrate, the structures of both the apo enzyme and the L116A mutant protein/DNA complex with severely decreased binding affinity were determined. (washington.edu)
  • Ami-noacyl compounds may be stabilized as tRNA-esters or enzyme thioesters (pantetheine-mediated peptide synthesis), while CoA-derivatives of amino acids have not been observed. (springer.com)
  • Proteins whose genes are observed to be correlated in expression, across a large number of experiments. (string-db.org)
  • To date, the genes encoding three eIF-2a protein kinases have been cloned and characterized. (elsevier.com)
  • Functional analysis of the metagenome of spent engine oil (SEO)-contaminated agricultural soil (AB1) using the Kyoto Encyclopedia of Genes and Genomes (KEGG) GhostKOALA, Cluster of Orthologous Groups (COG) of proteins, the Carbohydrate-Active Enzymes (CAZy) database, and the NCBI's conserved domain database (CDD) revealed extensive metabolism of carbohydrates via diverse carbohydrate-active enzymes and genes. (springeropen.com)
  • We have been able to elucidate the function of various hypothetical proteins and identify various missing genes. (nii.ac.jp)
  • In these HR-GIs, we recurrently found conserved genes such as the β-subunit of DNA-directed RNA polymerase, regulatory sigma factors, the elongation factor Tu and ribosomal protein genes typically associated with the core genome. (biomedcentral.com)
  • We report here the complete genome sequence of the T. maritimum type strain NCIMB 2154 T . The genome consists of a 3,435,971-base pair circular chromosome with 2,866 predicted protein-coding genes. (frontiersin.org)
  • Peptide fragmentation data, acquired by post-source decay mass spectrometry, proved a more successful strategy for the putative identification of proteins using the T. gondii EST database and protein databases from other organisms. (edu.au)
  • Researchers speculate that impaired protein assembly disrupts mitochondrial energy production. (medlineplus.gov)
  • Konovalova S, Tyynismaa H. Mitochondrial aminoacyl-tRNA synthetases in human disease. (medlineplus.gov)
  • Schwenzer H, Zoll J, Florentz C, Sissler M. Pathogenic implications of human mitochondrial aminoacyl-tRNA synthetases. (medlineplus.gov)
  • Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Complex II of the respiratory chain, which is specifically involved in the oxidation of succinate, carries electrons from FADH to CoQ. (nih.gov)
  • Aminoacyl-tRNA synthetases (ARSs) are ubiquitously expressed enzymes responsible for ligating amino acids to cognate tRNA molecules. (nih.gov)
  • Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. (creativebiomart.net)
  • Aminoacyl-tRNA synthetases (AARSs) catalyze aminoacylation of tRNAs in the cytoplasm. (nih.gov)
  • It contains three structural motifs typical of class IIa aminoacyl transferases and two signature regions common to histidyl-tRNA synthetases. (afsbio.com)
  • The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. (ebi.ac.uk)
  • Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric [ PMID: 10673435 ]. (ebi.ac.uk)
  • Class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet fold flanked by alpha-helices [ PMID: 8364025 ], and are mostly dimeric or multimeric, containing at least three conserved regions [ PMID: 8274143 , PMID: 2053131 , PMID: 1852601 ]. (ebi.ac.uk)
  • However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. (ebi.ac.uk)
  • 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. (ebi.ac.uk)
  • Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c [ PMID: 10447505 ]. (ebi.ac.uk)
  • Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process. (ebi.ac.uk)
  • Aminoacyl-tRNA synthetases: versatile players in the changing theater of translation. (ebi.ac.uk)
  • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. (ebi.ac.uk)
  • Classes of aminoacyl-tRNA synthetases and the establishment of the genetic code. (ebi.ac.uk)
  • Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases. (ebi.ac.uk)
  • HARS is from the class II family of aminoacyl-tRNA synthetases. (arp1.com)
  • Phylogenetic analysis of aminoacyl-tRNA synthetases (aaRSs) of all 20specificities from completely sequenced bacterial, archaeal, andeukaryotic genomes reveals a complex evolutionary picture. (embl.de)
  • 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. (embl.de)
  • This DALR domain is found in cysteinyl-tRNA-synthetases. (embl-heidelberg.de)
  • This domain is the core catalytic domain of tRNA synthetases and includes glycyl, prolyl, seryl and threonyl tRNA synthetases. (xfam.org)
  • This domain is found mainly hydrophobic tRNA synthetases. (syshospital.org)
  • Histidine and derivatives are compounds containing cysteine or a derivative thereof resulting from reaction of cysteine at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom. (bovinedb.ca)
  • This study evaluates the role of histidine in patients with HARS Syndrome. (bioportfolio.com)
  • Despite the similar kinetics, differential scanning fluorimetry revealed that Y454S is less thermally stable than Wild Type HARS , and cells from Y454S patients grown at elevated temperatures demonstrate diminished levels of protein synthesis compared to those of Wild Type cells. (antikoerper-online.de)
  • Immunoprecipitation of HARS transfected lysate using anti-HARS MaxPab rabbit polyclonal antibody and Protein A Magnetic Bead ( U0007 ), and immunoblotted with HARS MaxPab mouse polyclonal antibody (B01) ( H00003035-B01 ). (acris-antibodies.com)
  • Search proteins in UniProtKB for this molecule. (uniprot.org)
  • The position of the amino-acid change on the UniProtKB canonical protein sequence. (expasy.org)
  • L-Histidine exists in all living species, ranging from bacteria to humans. (bovinedb.ca)
  • The invention also comprises proteins prepared using misaminoacylated tRNAs which can be utilized in pharmaceutical compositions for the treatment of diseases and disorders in humans and other mammals, and kits which may be used for the detection of diseases and disorders. (google.ca)
  • While most protein synthesis occurs in the fluid surrounding the nucleus (cytoplasm), some proteins are synthesized in the mitochondria. (medlineplus.gov)
  • During protein synthesis, in either the mitochondria or the cytoplasm, a type of RNA called transfer RNA (tRNA) helps assemble protein building blocks (amino acids) into a chain that forms the protein. (medlineplus.gov)
  • L-Histidine exists as a solid, possibly soluble (in water), and a very strong basic compound (based on its pKa) molecule. (bovinedb.ca)
  • 10. The method of claim 1 wherein the tRNA molecule is aminoacylated by chemical misaminoacylation. (google.ca)
  • In modern living things, RNA is still the only molecule which functions both as a genotype (a genetic code) and phenotype (determining outward appearance-many RNAs are functional by themselves and are never converted to protein). (sunyorange.edu)
  • The N-terminal half (domains 1 and 2) contains the 'Rossman fold' typical for class I ligases and resembles the corresponding part of Escherichia coli GlnRS, whereas the C-terminal half exhibits a GluRS-specific structure [ PMID: 9426192 ]. (ebi.ac.uk)
  • Polyhistidine-tags are often used for affinity purification of polyhistidine-tagged recombinant proteins expressed in Escherichia coli and other prokaryotic expression systems. (wikipedia.org)
  • Methods The plasmid pSMT-EF4 encoding Mycobacterium tuberculosis EF4 protein was transformed into Escherichia coli ( E. coli) BL21 to make it express EF4 protein. (bvsalud.org)
  • Modulates proteasomal degradation of target proteins by the SCF (SKP2-CUL1-F-box protein) E3 ubiquitin-protein ligase complex. (drugbank.ca)
  • As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. (string-db.org)
  • Subsequent studies have revealed that among amino acids constituting proteins, histidine is strongly involved in the coordinate bond with metal ions. (wikipedia.org)
  • tRNA molecules are misaminoacylated with non-radioactive markers which may be non-native amino acids, amino acid analogs. (google.ca)
  • tRNA molecules are misaminoacylated with non-radioactive markers which may be non-native amino acids, amino acid analogs or derivatives, or substances recognized by the protein synthesizing machinery. (google.ca)
  • It had been thought that RNA could not perform the functions of proteins because the 4 RNA bases could not replace the important reacting parts (functional groups) of amino acids. (sunyorange.edu)
  • EC:6.1.1.17 ) is a class Ic ligase and shows several similarities with glutamate-tRNA ligase concerning structure and catalytic properties. (ebi.ac.uk)
  • Each aaRS contains a catalytic central domain (CCD), responsible for activating amino acid, and an anticodon-binding domain (ABD), necessary for binding the anticodon in cognate tRNA. (embl.de)
  • At this stage, raw lysate contains the recombinant protein among many other proteins originating from the bacterial host. (wikipedia.org)
  • Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase, as well as Met-AMP, His-AMP and Asp-AMP, lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) and AMP-N-alanine methyl ester. (drugbank.ca)
  • This organism, like Neisseria gonorrhoeae, is naturally competent, and protein complexes at the cell surface recognize the uptake signal sequence in extracellular DNA, an 8mer that is found at high frequency in Neisseria chromosomal DNA. (up.ac.za)
  • In the post-genomic era, proteomic studies analyzing the protein complement of a genome in a particular organism at any given time, have gained real significance. (usf.edu)
  • To date one crystal structure of a glutamate-tRNA ligase (Thermus thermophilus) has been solved. (ebi.ac.uk)
  • L-Lysine is a base, as are arginine and histidine. (drugbank.ca)
  • Proteins of the herpes simplex virus are rich in L-arginine, and tissue culture studies indicate an enhancing effect on viral replication when the amino acid ratio of L-arginine to L-lysine is high in the tissue culture media. (drugbank.ca)
  • From Arginine (R) to Histidine (H) at position 329 (R329H, p.Arg329His). (expasy.org)
  • The suf operon from cyanobacterium Anabaena PCC 7120 showed the presence of a cysteine desulfurase, sufS (alr2495), but not the accessory sulfur-accepting protein (SufE). (medworm.com)
  • Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed. (uniprot.org)
  • These proteins differ widely in size and oligomeric state, and have limited sequence homology [ PMID: 2203971 ]. (ebi.ac.uk)
  • Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown. (expasy.org)
  • A numberof euryarchaeal synapomorphies (unique shared characters) were identified;these are protein families that possess sequence signatures or domainarchitectures that are conserved in all euryarchaea but are not found inbacteria or eukaryotes. (embl-heidelberg.de)
  • The Fur proteins of Vibrio anguillarum , Vibrio cholerae , and Vibrio vulnificus are very highly related, although they share only about 60% of their polynucleotide sequence with that of E. coli , while the Fur protein of Yersinia pestis is highly similar to Fur from E. coli and other enteric bacteria ( 25 , 26 , 83 , 117 , 132 ). (asm.org)
  • Phosphorylation of the a subunit of cukaryotic initiation factor-2 (eIF-2) regulates protein synthesis in response to environmental stresses. (elsevier.com)
  • Respiratory electron transport, ATP synthesis by chemiosmotic coupling, and heat production by uncoupling proteins. (nih.gov)
  • This was conducted during post-exponential and stationary phases of growth so as to understand its adaptation over time by utilizing differential protein synthesis. (usf.edu)
  • Journal Article] A highly productive system for cell-free protein synthesis using a lysate of the hyperthermophilic archaeon, Thermococcus kodakaraensis. (nii.ac.jp)
  • A collection of articles that focus on an array of different scientific topics such as pathways, cancer, transmembrane proteins. (cusabio.com)
  • In cattle, L-histidine is involved in a couple of metabolic pathways, which include the histidine metabolism pathway and the beta-alanine metabolism pathway. (bovinedb.ca)
  • Aminoacyl-tRNAsynthetases are a class of enzymes that charge tRNAs with their cognate aminoacids. (creative-diagnostics.com)
  • Adsorption: Immunoaffinity adsorbed using insolubilized antigens as required to eliminate antibody activity reacting with other components of the immunoglobulin system and to any other serum protein. (mybiosource.com)
  • Therefore, if a number of histidines are added to the end of the protein by genetic engineering, the affinity of the protein for the metal ion is remarkably increased and the basic idea is that purification can be easily carried out. (wikipedia.org)
  • Could RNA molecules have performed the functions of proteins while simultaneously serving as the first genetic code? (sunyorange.edu)
  • These activities modify the ends of a nicked tRNA generated by a bacterial response to infection and facilitate their repair by T4 RNA ligase. (washington.edu)
  • Blumberg, P.M., Strominger, J.L.: Interaction of penicillin with the bacterial cell: Penicillin-binding proteins and penicillin-sensitive enzymes. (springer.com)