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
1984
Transfer RNA mischarging mediated by a mutant Escherichia coli glutaminyl-tRNA synthetase.
Inokuchi H, Hoben P, Yamao F, Ozeki H, Söll D. Transfer RNA mischarging mediated by a mutant Escherichia coli glutaminyl-tRNA synthetase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1984, 81: 5076-5080. PMID: 6382258, PMCID: PMC391640, DOI: 10.1073/pnas.81.16.5076.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseGlnS geneEscherichia coli glutaminyl-tRNA synthetaseAminoacyl-tRNA synthetase genesEarlier genetic studiesAmber suppressor tRNAWild-type enzymeSynthetase geneTRNA speciesAmber anticodonAmber mutationMutant tRNAsSuppressor tRNAGene productsAltered specificityGln mutantMutant geneTransducing phageEnzyme structureGenetic studiesTRNAGenesMischargingBiochemical meansAminoacylation reaction
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