1994
Recognition in the Glutamine tRNA System: from Structure to Function
Sherman J, Rogers M, Söll D. Recognition in the Glutamine tRNA System: from Structure to Function. 1994, 395-409. DOI: 10.1128/9781555818333.ch19.Peer-Reviewed Original ResearchEscherichia coli glutaminyl-tRNA synthetaseFirst high-resolution crystal structureAccurate protein synthesisProtein-RNA interactionsImportant specificity determinantsProtein-RNA complexesClose evolutionary relationshipE. coli GlnRSGlutaminyl-tRNA synthetaseHigh-resolution crystal structuresGlutamyl-tRNA synthetaseAminoacyl-tRNA synthetasesRecognition of tRNAEvolutionary relationshipsTRNA identity elementsTight recognitionSpecificity determinantsTRNA substratesGlnRBiochemical approachesCognate tRNATRNA systemTRNABiophysical techniquesEnzyme mechanismFunctional 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: 5201-5208. 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 ISynthetaseSelectivity and specificity in the recognition of tRNA by E coli glutaminyl-tRNA synthetase
Rogers M, Weygand-Durašević I, Schwob E, Sherman J, Rogers K, Adachi T, Inokuchi H, Söll D. Selectivity and specificity in the recognition of tRNA by E coli glutaminyl-tRNA synthetase. Biochimie 1993, 75: 1083-1090. PMID: 8199243, DOI: 10.1016/0300-9084(93)90007-f.Peer-Reviewed Original ResearchConceptsOpal suppressor tRNAGlutaminyl-tRNA synthetaseAcceptor stem recognitionSuppressor tRNAEscherichia coli glutaminyl-tRNA synthetaseGenetic selectionAmber suppressor tRNAExtensive mutational analysisRecognition of tRNARNA contactsTRNA transcriptsRelaxed specificityMutational analysisTRNAGlnRAcceptor stemExtensive proteinIndividual functional groupsMutantsSpecific recognitionAnticodonAminoacylationSynthetaseIdentity elementSynthetasesSpecificity in RNA: Protein Interactions; the Recognition of Escherichia Coli Glutamine tRNA
Rogers M, Weygand-Durašević I, Schwob E, Sherman J, Rogers K, Thomann H, Sylvers L, Jahn M, Inokuchi H, Ohtsuka E, Söll D. Specificity in RNA: Protein Interactions; the Recognition of Escherichia Coli Glutamine tRNA. 1993, 47-58. DOI: 10.1007/978-1-4615-2407-6_5.Peer-Reviewed Original ResearchProtein interactionsEscherichia coli glutaminyl-tRNA synthetaseRNA-protein structuresRole of tRNAGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetaseCognate aminoacyl-tRNA synthetaseRecognition of tRNAGenetic codeGlutamine tRNAAccuracy of translationRNA structureTRNABiophysical techniquesProtein synthesisMolecular levelMetabolic functionsAminoacyl-tRNA synthetase systemsCurrent understandingRNASynthetase systemSynthetaseUnusual elementsInteractionVariety
1990
Inaccuracy and the Recognition of †RNA
Rogers M, Soll D. Inaccuracy and the Recognition of †RNA. Progress In Nucleic Acid Research And Molecular Biology 1990, 39: 185-208. PMID: 2247608, DOI: 10.1016/s0079-6603(08)60627-3.Peer-Reviewed Original ResearchConceptsATP-dependent stepNoncognate aminoacyl-tRNAsGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetasesRecognition of tRNAAmber mutationGlnRAminoacyl-tRNAEditing mechanismTRNAMutantsMischargingCentral roleEnzymeSynthetasesMisaminoacylationSupF.SupFSynthetaseMutationsGlutamineMechanismSuppressionAssays