1996
Aminoacyl-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
1995
Divergence of glutamate and glutamine aminoacylation pathways: Providing the evolutionary rationale for mischarging
Rogers K, Söll D. Divergence of glutamate and glutamine aminoacylation pathways: Providing the evolutionary rationale for mischarging. Journal Of Molecular Evolution 1995, 40: 476-481. PMID: 7783222, DOI: 10.1007/bf00166615.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseGlutamine tRNAEukaryotic organismsProkaryotic organismsGln-tRNAGlnHorizontal gene transfer eventsGene transfer eventsGlutaminyl-tRNA synthetasesGram-negative eubacteriaGlutamyl-tRNA synthetaseAminoacyl-tRNA synthetasesAminoacyl-tRNA synthetaseFamily of enzymesEukaryotic organellesPool of glutamateAminoacyl-tRNATRNADifferent cellular mechanismsEvolutionary rationaleProtein synthesisOrganismsAmino acidsTransfer eventsCellular mechanismsSynthetase
1993
Specificity 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
1992
Synthetase competition and tRNA context determine the in vivo identity of tRNA discriminator mutants
Sherman J, Rogers K, Rogers M, Söll D. Synthetase competition and tRNA context determine the in vivo identity of tRNA discriminator mutants. Journal Of Molecular Biology 1992, 228: 1055-1062. PMID: 1474577, DOI: 10.1016/0022-2836(92)90314-a.Peer-Reviewed Original ResearchConceptsAmber suppressorTyrosine tRNAN-terminal protein sequencingGlutamyl-tRNA synthetaseE. coli dihydrofolate reductaseAminoacyl-tRNA synthetasesEffects of mutationsEfficiency of aminoacylationColi dihydrofolate reductaseSite of aminoacylationTyrosine specificityTRNAs exhibitGlutamine tRNAMutagenic analysisProtein sequencingGlutamate tRNAImportant identity elementVivo identityTRNANucleotide substitutionsTRNA identityDiscriminator baseDihydrofolate reductaseMultiple mutationsSynthetases