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Amino Acyl-tRNA SynthetasesRNA, Transfer, Amino AcylRNA, TransferUbiquitin-Protein LigasesMolecular Sequence DataProtein BiosynthesisDNA LigasesAminoacylationtRNA MethyltransferasesAnticodonIsoleucine-tRNA LigaseSKP Cullin F-Box Protein LigasesRNA, Transfer, Amino Acid-SpecificRNA, Transfer, PheTransfer RNA AminoacylationEscherichia coliNucleic Acid ConformationCullin ProteinsValine-tRNA LigasePeptide SynthasesUbiquitinationRNA, Transfer, IleBase SequencePolynucleotide LigasesRNA, Transfer, MetRibosomesAdenosine MonophosphateAspartate-tRNA LigaseSerine-tRNA LigaseUbiquitinRNA, BacterialRNA, Transfer, SerRNA Ligase (ATP)Phenylalanine-tRNA LigaseRING Finger DomainsAcylationCoenzyme A LigasesLysine-tRNA LigasePeptide Elongation Factor TuAmino Acid SequenceSubstrate SpecificitySporosarcinaPhenylalanineUbiquitin-Conjugating EnzymesBinding SitesRNA, Transfer, TrpIsoleucineRNA, Transfer, ArgCodonKineticsRNA, Transfer, GlyAmino AcidsMutationRNA, Transfer, AlaRNA, Transfer, GluTyrosine-tRNA LigaseModels, MolecularRNA, Transfer, AspPeptide Elongation FactorsHistidine-tRNA LigaseProtein BindingRNA, Transfer, ValSaccharomyces cerevisiaePeptide Chain Elongation, TranslationalPeptide BiosynthesisProtein Structure, TertiaryGlycine-tRNA LigaseRNA, Transfer, GlnRNA, Transfer, ProRNA, Transfer, HisCatalysisF-Box ProteinsPuromycinEndosomal Sorting Complexes Required for TransportSequence Homology, Amino AcidUbiquitinsProteasome Endopeptidase ComplexRNA, Transfer, ThrHydrolysisSequence AlignmentRNAAdenosine TriphosphateMagnesiumRNA EditingBacterial ProteinsEscherichia coli ProteinsUbiquitin-Protein Ligase ComplexesCatalytic DomainPolyubiquitinThiouridineRNA, Transfer, CysStructure-Activity RelationshipDiphosphatesPhylogenyRNA, FungalPeptidyl TransferasesGuanosine TriphosphateAmino Acid IsomerasesGenetic CodeUbiquitin-Activating Enzymes
SynthetaseAminoacylationCarbon-oxygenActivityCognateEnzymesMolecularAcceptorSaccharomycesEnzymeAnticodonResiduesSubstratesDiphosphateAttachmentAdenosineCrystal structureProteinsReactionsClassBelongsTerminalStructuresIsoleucyl-tRNA synthThreonyl-tRNA synthetaseTryptophanyl-tRNA synthetaseTyrosine-tRNA LThreonine--tRNANucleotideSynthesisMultifunctionalTyrosyl-tRNA synthetaseCytoplasmicAspartyl-tRNA synthetaseSynthetase familyThermusAminoacylation of tRNAMitochondrialGeneLysyl-tRNAAmino-acylGenesSpecific amino acidMoleculeMoietyThrRSYARSCatalyzesTranslationAdenosine
Synthetase19
  • Tyrosine-tRNA ligase (EC 6.1.1.1), also known as tyrosyl-tRNA synthetase is an enzyme that is encoded by the gene YARS. (wikipedia.org)
  • Tyrosyl-tRNA synthetase from Bacillus stearothermophilus was the first synthetase whose crystal structure has been solved at high resolution (2.3 Å), alone or in complex with tyrosine, tyrosyl-adenylate or tyrosinyl-adenylate. (wikipedia.org)
  • Leucyl-tRNA synthetase catalyzes attachment of leucine amino acid to its cognate tRNA. (nih.gov)
  • This domain is found at the amino terminus of Arginyl tRNA synthetase, also called additional domain 1 (Add-1). (embl-heidelberg.de)
  • Crystal structure of arginyl-tRNA synthetase from Klebsiella pneumoniae subsp. (embl-heidelberg.de)
  • Cloning and characterization of the gene coding for cytoplasmic seryl-tRNA synthetase from Saccharomyces cerevisiae. (ymdb.ca)
  • The human alanyl-tRNA synthetase (AARS) belongs to a family of tRNA synthases, of the class II enzymes. (nih.gov)
  • A humanized yeast model reveals dominant-negative properties of neuropathy-associated alanyl-tRNA synthetase mutations. (nih.gov)
  • Alanyl-tRNA synthetase 1 (AARS1) gene mutation in a family with intermediate Charcot-Marie-Tooth neuropathy. (nih.gov)
  • The Plasmodium genome encodes two forms of prolyl-tRNA synthetase, one found in the cytoplasm (PfcPRS, described here) and one in the apicoplast (PfaPRS, encoded by PF3D7_0925300 ). (guidetomalariapharmacology.org)
  • Class II Histidinyl-tRNA synthetase (HisRS)-like. (ntu.edu.sg)
  • The DARS1 gene provides instructions for making an enzyme called aspartyl-tRNA synthetase. (medlineplus.gov)
  • Enzymes called aminoacyl-tRNA synthetases, including aspartyl-tRNA synthetase, attach a particular amino acid to a specific tRNA. (medlineplus.gov)
  • Aspartyl-tRNA synthetase attaches the amino acid aspartate to the correct tRNA, which helps ensure that aspartate is added at the proper place in proteins. (medlineplus.gov)
  • In addition to its role in protein synthesis, aspartyl-tRNA synthetase may have other functions that are not fully understood. (medlineplus.gov)
  • Most of the mutations in the DARS1 gene change single amino acids in the aspartyl-tRNA synthetase enzyme. (medlineplus.gov)
  • Researchers do not understand why reduced activity of aspartyl-tRNA synthetase affects myelination or why specific parts of the brainstem and spinal cord are involved. (medlineplus.gov)
  • Park SG, Choi EC, Kim S. Aminoacyl-tRNA synthetase-interacting multifunctional proteins (AIMPs): a triad for cellular homeostasis. (medlineplus.gov)
  • GARS is a glycyl-tRNA synthetase, one of the aminoacyl-tRNA synthetases that charge tRNAs with their cognate amino acids. (thermofisher.com)
Aminoacylation3
  • These latter enzymes link amino acids to their cognate transfer RNAs (tRNA) in aminoacylation reactions that establish the connection between a specific amino acid and a nucleotide triplet anticodon embedded in the tRNA. (wikipedia.org)
  • Mutagenesis experiments have shown that the flexibility of the peptide that links the α-ACB and S4-like domains is responsible for the disorder of the latter in the structure and that elements of sequence in this linker peptide are essential for the binding of tRNA(Tyr) by YARS and its aminoacylation with tyrosine. (wikipedia.org)
  • Predicted to be involved in isoleucyl-tRNA aminoacylation and mitochondrial translation. (mcw.edu)
Carbon-oxygen1
  • This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in tRNA and related compounds. (wikipedia.org)
Activity1
Cognate1
  • tRNA synthases are the enzymes that interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. (nih.gov)
Enzymes1
  • As of late 2007, 34 structures have been solved for this class of enzymes, with PDB accession codes The tyrosyl-tRNA synthetases (YARS) are either homodimers or monomers with a pseudo-dimeric structure. (wikipedia.org)
Molecular1
  • In this work, we have investigated the aminoacetylation step catalyzed by leucyl-tRNA synthase, using ab initio quantum chemical/molecular mechanical hybrid potentials in conjunction with reaction-path-location algorithms and molecular dynamics free energy simulations. (nih.gov)
Acceptor1
  • They consist of a catalytic domain which interacts with the amino acid acceptor-T psi C helix of the tRNA, and a second domain which interacts with the rest of the tRNA structure. (nih.gov)
Saccharomyces1
Enzyme3
  • Tyrosine-tRNA ligase catalyzes the chemical reaction ATP + L-tyrosine + tRNA(Tyr) ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + L-tyrosyl-tRNA(Tyr) The three substrates of this enzyme are ATP, L-tyrosine, and a tyrosine-specific transfer RNA [tRNA(Tyr) or tRNATyr], whereas its three products are AMP, diphosphate, and L-tyrosyl-tRNA(Tyr). (wikipedia.org)
  • These alterations occur in a region of the enzyme called the active site, where aspartate and the tRNA come together so the amino acid can be transferred. (medlineplus.gov)
  • The altered enzyme has difficulty adding the amino acid to the tRNA, which in turn hinders the addition of aspartate to proteins. (medlineplus.gov)
Anticodon1
  • The C-terminal moiety of the YARSs varies in sequence, length and organization and is involved in the recognition of the tRNA anticodon. (wikipedia.org)
Residues2
  • We invoke various groups as potential proton acceptors-namely, the phosphate and leucyl amino groups of leucyl-adenylate, the A76 base of tRNA, and the Asp80 and Glu532 residues of the protein-and consider both metal-assisted and metal-free reactions. (nih.gov)
  • It is about 140 residues long and it has been suggested that this domain will be involved in tRNA recognition. (embl-heidelberg.de)
Substrates1
  • Rabbit polyclonal to YARS2.The fidelity of protein synthesis requires efficient discrimination of amino acid substrates byaminoacyl-tRNA synthetases. (arqueologiamendoza.com)
Diphosphate1
  • Catalysis of the reaction: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). (umassmed.edu)
Attachment1
  • Catalyzes the attachment of serine to tRNA(Ser). (ymdb.ca)
Adenosine1
  • During the second, aminoacetylation, step of the reaction, the leucyl moiety is transferred from leucyl-adenylate to the terminal A76 adenosine of tRNA. (nih.gov)
Crystal structure2
  • A structural model of the complex between B. sterothermophilus YARS and tRNA(Tyr) was constructed using extensive mutagenesis data on both YARS and tRNATyr and found consistent with the crystal structure of the complex between YARS and tRNA(Tyr) from Thermus thermophilus, which was subsequently solved at 2.9 Å resolution. (wikipedia.org)
  • The crystal structure of the complex between YARS from Methanococcus jannaschii, tRNA(Tyr) and L-tyrosine has been solved at 1.95 Å resolution. (wikipedia.org)
Proteins4
  • There are 26085 Arg_tRNA_synt_N domains in 26083 proteins in SMART's nrdb database. (embl-heidelberg.de)
  • Taxonomic distribution of proteins containing Arg_tRNA_synt_N domain. (embl-heidelberg.de)
  • The complete taxonomic breakdown of all proteins with Arg_tRNA_synt_N domain is also avaliable . (embl-heidelberg.de)
  • Click on the protein counts, or double click on taxonomic names to display all proteins containing Arg_tRNA_synt_N domain in the selected taxonomic class. (embl-heidelberg.de)
Reactions1
  • 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. (embl-heidelberg.de)
Class4
  • iv) the two signature sequences HIGH and KMSKS of the class I aminoacyl-tRNA synthetases. (wikipedia.org)
  • However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. (embl-heidelberg.de)
  • Class II tRNA synthases evolved early in evolution and are highly conserved. (nih.gov)
  • This protein is an (alpha)2 dimer which belongs to the class II family of tRNA synthetases. (thermofisher.com)
Belongs1
  • More specifically, it belongs to the family of the aminoacyl-tRNA synthetases. (wikipedia.org)
Terminal1
  • it shares strong homology with the C-terminal domain of the tryptophanyl-tRNA synthetases and was therefore named C-W/Y domain. (wikipedia.org)
Structures2
  • The crystal structures of several archaeal tyrosyl-tRNA synthetases are available. (wikipedia.org)
  • Comparisons of primary, secondary and tertiary structures supported the hypothesis that protein kinases and choline kinases evolved from an ancient aminoacyl-tRNA ligase. (dissertation.com)
Isoleucyl-tRNA synth2
  • Interaction of EPRS with hsp90 was targeted to the region of three tandem repeats linking the two catalytic domains of EPRS that is also responsible for the interaction with isoleucyl-tRNA synthetase (IRS). (korea.ac.kr)
  • The correct amino acid sequence of E. coli isoleucyl-tRNA synthetase (IleRS) was established by means of peptide mapping by MALDI mass spectrometry, using a set of four endoproteases (trypsin, LysC, AspN and GluC). (openbiochemistryjournal.com)
Threonyl-tRNA synthetase4
  • E. coli threonyl-tRNA synthetase (ThrRS) is a class II enzyme that represses the translation of its own mRNA. (proteopedia.org)
  • The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site. (proteopedia.org)
  • Sankaranarayanan R, Dock-Bregeon AC, Romby P, Caillet J, Springer M, Rees B, Ehresmann C, Ehresmann B, Moras D. The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site. (proteopedia.org)
  • Autoantibodies to histidyl-tRNA synthetase (HisRS) or to alanyl-, asparaginyl-, glycyl-, isoleucyl-, or threonyl-tRNA synthetase occur in approximately 25% of patients with polymyositis or dermatomyositis. (mcw.edu)
Tryptophanyl-tRNA synthetase4
  • We deleted the anticodon binding domain from tryptophanyl-tRNA synthetase and fused the discontinuous segments comprising its active site. (nyu.edu)
  • Two forms of tryptophanyl-tRNA synthetase exist, a cytoplasmic form, named WARS, and a mitochondrial form, named WARS2. (nih.gov)
  • Tryptophanyl-tRNA synthetase (WARS) catalyzes the aminoacylation of tRNA(trp) with tryptophan and is induced by interferon. (nih.gov)
  • Tryptophanyl-tRNA synthetase belongs to the class I tRNA synthetase family. (nih.gov)
Tyrosine-tRNA L2
  • Tyrosine-tRNA ligase (EC 6.1.1.1), also known as tyrosyl-tRNA synthetase is an enzyme that is encoded by the gene YARS. (wikipedia.org)
  • Tyrosine-tRNA ligase catalyzes the chemical reaction ATP + L-tyrosine + tRNA(Tyr) ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + L-tyrosyl-tRNA(Tyr) The three substrates of this enzyme are ATP, L-tyrosine, and a tyrosine-specific transfer RNA [tRNA(Tyr) or tRNATyr], whereas its three products are AMP, diphosphate, and L-tyrosyl-tRNA(Tyr). (wikipedia.org)
Threonine--tRNA1
  • threonine-tRNA ligase [Cryptococcus neoformans var. (uma.es)
Nucleotide1
  • Because of their central role in linking amino acids with nucleotide triplets contained in tRNAS, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. (thermofisher.com)
Synthesis6
  • While the required tRNAs and rRNAs are produced by transcription of the mitochondrial genome, all other factors needed for protein synthesis are synthesized in the cytosol and imported. (nih.gov)
  • The aminoacyl-tRNA synthetases (aaRSs) are a large and diverse enzyme family with an essential role in the ATP-dependent aminoacylation of cognate tRNAs with their respective amino acids for use in protein synthesis [ 2 ]. (guidetoimmunopharmacology.org)
  • 2. Ibba M, Soll D. (2000) Aminoacyl-tRNA synthesis. (guidetoimmunopharmacology.org)
  • In addition to its role in protein synthesis, aspartyl-tRNA synthetase may have other functions that are not fully understood. (medlineplus.gov)
  • The synthesis of aminoacyl tRNA by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA, to be used in ribosome-mediated polypeptide synthesis. (systemsbiology.net)
  • Studies with such altered RNAs provided greater insights into the specificity of amino acyl tRNA synthesis and utilization in protein biosynthesis. (nih.gov)
Multifunctional2
  • Park SG, Choi EC, Kim S. Aminoacyl-tRNA synthetase-interacting multifunctional proteins (AIMPs): a triad for cellular homeostasis. (medlineplus.gov)
  • Aminoacyl-tRNA synthetase complicated interacting multifunctional proteins-2 (AIMP2), also called JTV-1 or P38, is certainly a parkin substrate that's within Lewy body inclusions of Parkinsons disease substantia nigra17,18. (monossabios.com)
Tyrosyl-tRNA synthetase1
  • Tyrosyl-tRNA synthetase from Bacillus stearothermophilus was the first synthetase whose crystal structure has been solved at high resolution (2.3 Å), alone or in complex with tyrosine, tyrosyl-adenylate or tyrosinyl-adenylate. (wikipedia.org)
Cytoplasmic1
Aspartyl-tRNA synthetase6
  • acetylated processed McC no longer inhibits aspartyl-tRNA synthetase. (medscape.com)
  • [ 31 ] Acetylation of the α-amino group of the amino acid adenylate would both disrupt favorable hydrogen bond interactions and result in steric clashes with the backbone of aspartyl-tRNA synthetase, which provides structural rationale for MccE CTD protective function. (medscape.com)
  • The DARS1 gene provides instructions for making an enzyme called aspartyl-tRNA synthetase. (medlineplus.gov)
  • Aspartyl-tRNA synthetase attaches the amino acid aspartate to the correct tRNA, which helps ensure that aspartate is added at the proper place in proteins. (medlineplus.gov)
  • Most of the mutations in the DARS1 gene change single amino acids in the aspartyl-tRNA synthetase enzyme. (medlineplus.gov)
  • Researchers do not understand why reduced activity of aspartyl-tRNA synthetase affects myelination or why specific parts of the brainstem and spinal cord are involved. (medlineplus.gov)
Synthetase family1
  • Isoleucine-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family and has been identified as a target of autoantibodies in the autoimmune disease polymyositis/dermatomyositis. (thermofisher.com)
Thermus1
  • A structural model of the complex between B. sterothermophilus YARS and tRNA(Tyr) was constructed using extensive mutagenesis data on both YARS and tRNATyr and found consistent with the crystal structure of the complex between YARS and tRNA(Tyr) from Thermus thermophilus, which was subsequently solved at 2.9 Å resolution. (wikipedia.org)
Aminoacylation of tRNA2
Mitochondrial2
  • Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs. (nih.gov)
  • This gene produces a mitochondrial methionyl-tRNA synthetase protein that is encoded by the nuclear genome and imported to the mitochondrion. (nih.gov)
Gene1
  • This gene encodes a protein which contains a ferredoxin-fold anticodon-binding domain which is contained in a subset of phenylalanyl tRNA synthetases. (nih.gov)
Lysyl-tRNA1
  • Nonautoantigenic aspartyl-tRNA and lysyl-tRNA synthetases were not chemotactic. (mcw.edu)
Amino-acyl2
Genes1
  • Genes for the remaining missing synthetases were also found with the exception of glutaminyl-tRNA synthetase. (nih.gov)
Specific amino acid1
  • A type of RNA called transfer RNA (tRNA) carries a specific amino acid to the growing chain. (medlineplus.gov)
Molecule1
  • The April 2001 RCSB PDB Molecule of the Month feature on Aminoacyl-tRNA Synthetases by David S. Goodsell is 10.2210/rcsb_pdb/mom_2001_4 . (proteopedia.org)
Moiety3
  • The C-terminal moiety of the YARSs varies in sequence, length and organization and is involved in the recognition of the tRNA anticodon. (wikipedia.org)
  • Only minimal contacts are made with the aminoacyl moiety of the substrate. (medscape.com)
  • Altogether, the oxidized 3'-end of tRNA Ile and the pyridoxal moiety of the ATP analog ADP-PL react with the lysyl residues 601 and 604 of the consensus sequence 601 KMSKS 605 . (openbiochemistryjournal.com)
ThrRS1
  • We report the crystal structure at 2.9 A resolution of the complex between tRNA(Thr) and ThrRS, whose structural features reveal novel strategies for providing specificity in tRNA selection. (proteopedia.org)
YARS3
  • Mutagenesis experiments have shown that the flexibility of the peptide that links the α-ACB and S4-like domains is responsible for the disorder of the latter in the structure and that elements of sequence in this linker peptide are essential for the binding of tRNA(Tyr) by YARS and its aminoacylation with tyrosine. (wikipedia.org)
  • The crystal structure of the complex between YARS from Methanococcus jannaschii, tRNA(Tyr) and L-tyrosine has been solved at 1.95 Å resolution. (wikipedia.org)
  • The structure of the complex between YARS from Saccharomyces cerevisiae, tRNA(Tyr) and an analog of tysosyl-adenylate has been solved at 2.4 Å resolution. (wikipedia.org)
Catalyzes1
  • Catalyzes the attachment of serine to tRNA(Ser). (ymdb.ca)
Translation1
  • Aminoacyl-tRNA synthetases (ARSs) are critical for protein translation. (omeka.net)
Adenosine2
  • In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. (systemsbiology.net)
  • For the ATP binding site, the affinity labeling reagent was pyridoxal 5'-diphospho-5'-adenosine (ADP-PL), whereas periodate-oxidized tRNA Ile , the 2',3'-dialdehyde derivative of tRNA Ile was used to label the binding site for the 3'-end of tRNA on the synthetase. (openbiochemistryjournal.com)