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
The C-terminal Extension of Yeast Seryl-tRNA Synthetase Affects Stability of the Enzyme and Its Substrate Affinity (*)
Weygand-Durasevic I, Lenhard B, Filipic S, Söll D. The C-terminal Extension of Yeast Seryl-tRNA Synthetase Affects Stability of the Enzyme and Its Substrate Affinity (*). Journal Of Biological Chemistry 1996, 271: 2455-2461. PMID: 8576207, DOI: 10.1074/jbc.271.5.2455.Peer-Reviewed Original ResearchAminoacyl-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
1977
Suppression of a defective alanyl-tRNA synthetase in Escherichia coli: A compensatory mutation to high alanine affinity
Theall G, Low K, Söll D. Suppression of a defective alanyl-tRNA synthetase in Escherichia coli: A compensatory mutation to high alanine affinity. Molecular Genetics And Genomics 1977, 156: 221-227. PMID: 340903, DOI: 10.1007/bf00283495.Peer-Reviewed Original ResearchConceptsTemperature-resistant revertantsAlanyl-tRNA synthetaseResistant revertantsE. coli mapWild-type enzymeRibosomal proteinsStructural geneGene mapsSynthetase mutantsMutant enzymesParental enzymeCompensatory mutationsTemperature-sensitive characterEscherichia coliAdditional mutationsEnzymeRevertantsSynthetaseMutationsKm valuesAlanineRecAMutantsGenesAffinity