1998
The Terminal Adenosine of tRNAGln Mediates tRNA-Dependent Amino Acid Recognition by Glutaminyl-tRNA Synthetase †
Liu J, Ibba M, Hong K, Söll D. The Terminal Adenosine of tRNAGln Mediates tRNA-Dependent Amino Acid Recognition by Glutaminyl-tRNA Synthetase †. Biochemistry 1998, 37: 9836-9842. PMID: 9657697, DOI: 10.1021/bi980704+.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseAmino acid recognitionEscherichia coli glutaminyl-tRNA synthetaseSequence-specific interactionsDouble-mutant cycle analysisAmino acid glutamineMutant cycle analysisApparent affinityConservative replacementsNonconservative replacementGlutamine bindingKcat/KmTyr211Biochemical studiesNoncognate tRNAsTerminal adenosineSynthetaseGlutamineSpecific interactionsCycle analysisKmAsp66AffinityTRNADramatic decrease
1996
Interactions between tRNA identity nucleotides and their recognition sites in glutaminyl-tRNA synthetase determine the cognate amino acid affinity of the enzyme.
Ibba M, Hong K, Sherman J, Sever S, Söll D. Interactions between tRNA identity nucleotides and their recognition sites in glutaminyl-tRNA synthetase determine the cognate amino acid affinity of the enzyme. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 6953-6958. PMID: 8692925, PMCID: PMC38915, DOI: 10.1073/pnas.93.14.6953.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesAnimalsBase SequenceBinding SitesCalorimetryCloning, MolecularConsensus SequenceEscherichia coliHumansKineticsModels, StructuralMolecular Sequence DataNucleic Acid ConformationProtein FoldingRecombinant ProteinsRNA, Transfer, GlnSequence Homology, Nucleic AcidConceptsGlutaminyl-tRNA synthetaseAmino acid affinityAmino acid recognitionEscherichia coli glutaminyl-tRNA synthetaseBase pairsIdentity nucleotidesProtein-RNA interactionsDiscriminator baseE. coli tryptophanyl-tRNA synthetaseAminoacyl-tRNA synthetasesSequence-specific interactionsAcid affinityRecognition sitesAbility of tRNATryptophanyl-tRNA synthetaseTRNA specificityNoncognate substratesTranslational fidelityTRNA recognitionBiochemical functionsRNA recognitionCognate tRNATRNAMajor binding siteNoncognate tRNAsGlutaminyl‐tRNA synthetase: from genetics to molecular recognition
Ibba M, Hong K, Söll D. Glutaminyl‐tRNA synthetase: from genetics to molecular recognition. Genes To Cells 1996, 1: 421-427. PMID: 9078373, DOI: 10.1046/j.1365-2443.1996.d01-255.x.Peer-Reviewed Original ResearchConceptsEscherichia coli glutaminyl-tRNA synthetaseMajority of tRNAsCorrect amino acidGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetasesSequence-specific interactionsAmino acid recognitionEfficiency of aminoacylationGenetic codeTRNA selectionGlnRTRNAAmino acidsNoncognate tRNAsCellular viabilityStructural studiesMolecular recognitionSynthetasesAminoacylationComplex displaysGeneticsSynthetaseGlutamineMechanismViabilityAminoacyl-tRNA Synthetases Optimize Both Cognate tRNA Recognition and Discrimination against Noncognate tRNAs †
Sherman J, Söll D. Aminoacyl-tRNA Synthetases Optimize Both Cognate tRNA Recognition and Discrimination against Noncognate tRNAs †. Biochemistry 1996, 35: 601-607. PMID: 8555233, DOI: 10.1021/bi951602b.Peer-Reviewed Original ResearchConceptsTRNA recognitionNoncognate tRNAsEscherichia coli glutaminyl-tRNA synthetaseWild-type GlnRSGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetasesNucleic acid interactionsGlutamine tRNAFirst base pairMutational analysisSpecific proteinsTRNAGlnRSequence preferenceMutantsBase pairsAcid interactionsDecreased affinityVivoTRNAGlnAffinitySynthetasesProteinSynthetaseCrystal structure
1993
Acceptor 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