2000
One Polypeptide with Two Aminoacyl-tRNA Synthetase Activities
Stathopoulos C, Li T, Longman R, Vothknecht U, Becker H, Ibba M, Söll D. One Polypeptide with Two Aminoacyl-tRNA Synthetase Activities. Science 2000, 287: 479-482. PMID: 10642548, DOI: 10.1126/science.287.5452.479.Peer-Reviewed Original ResearchConceptsProlyl-tRNA synthetaseProtein synthesisCysteinyl-tRNA synthetase activityAmino-terminal sequenceSynthetase activityAminoacyl-tRNA synthetase activityCertain archaeaEvolutionary originMethanococcus jannaschiiGenome sequenceSubstrate specificityGenetic analysisSuch organismsMessenger RNARNA synthetasesSynthetaseSequenceArchaeaJannaschiiSynthetasesRNAOrganismsPolypeptideProlylProtein
1994
Functional communication in the recognition of tRNA by Escherichia coli glutaminyl-tRNA synthetase.
Rogers M, Adachi T, Inokuchi H, Söll D. Functional communication in the recognition of tRNA by Escherichia coli glutaminyl-tRNA synthetase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 291-295. PMID: 7506418, PMCID: PMC42933, DOI: 10.1073/pnas.91.1.291.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acyl-tRNA SynthetasesAnticodonBacterial ProteinsEscherichia coliGenes, SuppressorModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein Structure, TertiaryRNA, BacterialRNA, TransferStructure-Activity RelationshipSubstrate SpecificityTransfer RNA AminoacylationConceptsEscherichia coli glutaminyl-tRNA synthetaseGlutaminyl-tRNA synthetaseLys-317Genetic selectionOpal suppressorMutant enzymesWild-type GlnRSAsp-235Anticodon-binding domainSingle amino acid changeSite-directed mutagenesisNumber of mutantsAmino acid changesRecognition of tRNAGlnR mutantAnticodon recognitionAdditional mutantsGln mutantGlnRMutantsAcid changesBase pairsSpecificity constantAminoacylationTRNA
1993
Selection of a 'minimal' glutaminyl-tRNA synthetase and the evolution of class I synthetases.
Schwob E, Söll D. Selection of a 'minimal' glutaminyl-tRNA synthetase and the evolution of class I synthetases. The EMBO Journal 1993, 12: 5201-8. PMID: 7505222, PMCID: PMC413784, DOI: 10.1002/j.1460-2075.1993.tb06215.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesBacterial ProteinsBase SequenceBinding SitesBiological EvolutionEscherichia coliModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein Structure, TertiaryRNA, BacterialRNA, Transfer, GlnRNA, Transfer, SerStructure-Activity RelationshipTransfer RNA AminoacylationConceptsGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetasesEscherichia coli glutaminyl-tRNA synthetaseClass I aminoacyl-tRNA synthetasesNew recognition specificitiesNon-catalytic domainSubstrate recognition propertiesNon-cognate tRNAsRecognition of tRNACommon ancestorSequence motifsAmber suppressorGenetic codeTRNA substratesCatalytic coreGlnRTRNARecognition specificityDistinct domainsEnzymatic activityElaborate relationshipSynthetasesSpecific roleClass ISynthetaseDiscrimination among tRNAs intermediate in glutamate and glutamine acceptor identity.
Rogers K, Söll D. Discrimination among tRNAs intermediate in glutamate and glutamine acceptor identity. Biochemistry 1993, 32: 14210-9. PMID: 7505112, DOI: 10.1021/bi00214a021.Peer-Reviewed Original ResearchAmino Acyl-tRNA SynthetasesAnticodonBase SequenceBiological EvolutionEscherichia coliGlutamate-tRNA LigaseHydrogen BondingKineticsMolecular Sequence DataNucleic Acid ConformationRNA, BacterialRNA, Transfer, GlnRNA, Transfer, GluStructure-Activity RelationshipSubstrate SpecificityTransfer RNA AminoacylationAcceptor end binding domain interactions ensure correct aminoacylation of transfer RNA.
Weygand-Durasević I, Schwob E, Söll D. Acceptor end binding domain interactions ensure correct aminoacylation of transfer RNA. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 2010-2014. PMID: 7680483, PMCID: PMC46010, DOI: 10.1073/pnas.90.5.2010.Peer-Reviewed Original ResearchConceptsAmber suppressor tRNASuppressor tRNAEscherichia coli glutaminyl-tRNA synthetaseAcceptor stemAccuracy of aminoacylationGlutaminyl-tRNA synthetaseWild-type enzymeNoncognate complexGlnR mutantTRNA specificityArg-130Amber mutationTransfer RNASuch mutantsMutant enzymesCritical residuesDomain contributesDomain interactionsRecognition specificityTRNAGlu-131MutantsNoncognate tRNAsGlnRCorrect aminoacylation
1992
Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation
Sherman J, Rogers M, Söll D. Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation. Nucleic Acids Research 1992, 20: 2847-2852. PMID: 1377381, PMCID: PMC336931, DOI: 10.1093/nar/20.11.2847.Peer-Reviewed Original ResearchConceptsAccuracy of aminoacylationAminoacyl-tRNA synthetasesTyrosyl-tRNA synthetaseE. coli tyrosyl-tRNA synthetaseEscherichia coli tyrosyl-tRNA synthetaseGlutaminyl-tRNA synthetaseLevel of aminoacylationProtein biosynthesisTRNASynthetasesAminoacylationCompetition assaysDiscriminator baseDifferent synthetasesConcurrent overexpressionCorrect aminoacylationSynthetaseFirst baseRelative affinityVivoMisacylationAssaysAnticodonBiosynthesisCompetition
1990
The accuracy of aminoacylation — ensuring the fidelity of the genetic code
Söll D. The accuracy of aminoacylation — ensuring the fidelity of the genetic code. Cellular And Molecular Life Sciences 1990, 46: 1089-1096. PMID: 2253707, DOI: 10.1007/bf01936918.Peer-Reviewed Original ResearchConceptsAccuracy of aminoacylationTransfer RNA speciesAminoacyl-tRNA synthetasesMessenger RNA codonRNA speciesProtein biosynthesisGenetic codeProtein interactionsParticular tRNATRNACorrect attachmentBiophysical techniquesRNA codonsAmino acidsSynthetasesSpecific recognitionProper interactionAnticodonBiosynthesisCodonAminoacylationNucleotidesSpeciesEnzymeIdentity element
1974
Covalent attachment of fluorescent groups to transfer ribonucleic acid. Reactions with 4-bromomethyl-7-methoxy-2-oxo-2H-benzopyran.
Yang C, Soell D. Covalent attachment of fluorescent groups to transfer ribonucleic acid. Reactions with 4-bromomethyl-7-methoxy-2-oxo-2H-benzopyran. Biochemistry 1974, 13: 3615-21. PMID: 4367729, DOI: 10.1021/bi00714a033.Peer-Reviewed Original ResearchAlkaline PhosphataseAmino Acyl-tRNA SynthetasesBenzopyransBromineCarbon RadioisotopesEscherichia coliFluorescenceFormatesGlutamatesMethionineMethyl EthersModels, ChemicalNucleosidesPhosphoric Diester HydrolasesPseudouridineRibonucleasesRNA, BacterialRNA, TransferSpectrometry, FluorescenceStructure-Activity RelationshipTransfer RNA AminoacylationUridineInvolvement of the anticodon region of Escherichia coli tRNAGln and tRNAGlu in the specific interaction with cognate aminoacyl-tRNA synthetase Alteration of the 2-thiouridine derivatives located in the anticodon of the tRNAs by BrCN or sulfur deprivation
Seno T, Agris P, Söll D. Involvement of the anticodon region of Escherichia coli tRNAGln and tRNAGlu in the specific interaction with cognate aminoacyl-tRNA synthetase Alteration of the 2-thiouridine derivatives located in the anticodon of the tRNAs by BrCN or sulfur deprivation. Biochimica Et Biophysica Acta 1974, 349: 328-338. PMID: 4366808, DOI: 10.1016/0005-2787(74)90120-8.Peer-Reviewed Original ResearchAdenosine TriphosphateAmino Acyl-tRNA SynthetasesCarbon RadioisotopesChromatography, Ion ExchangeCyanogen BromideDiphosphatesEscherichia coliGlutamatesGlutamineKineticsPhosphorus RadioisotopesProtein BiosynthesisRNA, BacterialRNA, TransferSpectrophotometry, UltravioletThiouridineTransfer RNA Aminoacylation