1994
Connecting Anticodon Recognition with the Active Site of Escherichia coli Glutaminyl-tRNA Synthetase
Weygand-Duraševic I, Rogers M, Söll D. Connecting Anticodon Recognition with the Active Site of Escherichia coli Glutaminyl-tRNA Synthetase. Journal Of Molecular Biology 1994, 240: 111-118. PMID: 8027995, DOI: 10.1006/jmbi.1994.1425.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseAnticodon recognitionMutant enzymesEscherichia coli glutaminyl-tRNA synthetaseOpal suppressor tRNASpecificity constantMutant gene productsWild-type enzymeAmino acid loopExtensive conformational changesActive siteNumber of mutationsSuppressor tRNAGene productsGlnRPathways of communicationSaturation mutagenesisTRNAAcceptor stemAcid loopGenetic selectionConformational changesAnticodonPoor substrateAminoacylationFunctional 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
1992
Recognition of bases in Escherichia coli tRNA(Gln) by glutaminyl‐tRNA synthetase: a complete identity set.
Hayase Y, Jahn M, Rogers M, Sylvers L, Koizumi M, Inoue H, Ohtsuka E, Söll D. Recognition of bases in Escherichia coli tRNA(Gln) by glutaminyl‐tRNA synthetase: a complete identity set. The EMBO Journal 1992, 11: 4159-4165. PMID: 1396597, PMCID: PMC556926, DOI: 10.1002/j.1460-2075.1992.tb05509.x.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseRecognition of basesSet of tRNAsEscherichia coliCognate aminoacyl-tRNA synthetasesAminoacyl-tRNA synthetasesCorrect aminoacylationRecombinant RNA technologySet of nucleotidesNumber of mutantsGlutamine identityTRNA genesTRNA discriminationTransfer RNAExcellent systemGlnRFunctional importanceSingle deletionSpecific contactsRNA technologyBase changesSpecificity constantAminoacylationSpecific guanosineMutants
1991
Anticodon and acceptor stem nucleotides in tRNAGln are major recognition elements for E. coli glutaminyl-tRNA synthetase
Jahn M, Rogers M, Söll D. Anticodon and acceptor stem nucleotides in tRNAGln are major recognition elements for E. coli glutaminyl-tRNA synthetase. Nature 1991, 352: 258-260. PMID: 1857423, DOI: 10.1038/352258a0.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseMutant tRNAsE. coli glutaminyl-tRNA synthetaseEfficient amber suppressorsAminoacyl-tRNA synthetasesCorresponding transfer RNASet of nucleotidesMajor recognition elementGlutamine identityAcceptor stem regionTRNA discriminationTransfer RNAAmber suppressorProtein biosynthesisTRNA moleculesUnmodified tRNACorrect attachmentAnticodon regionTRNAAcceptor stemSimilar kinetic parametersEscherichia coliAmino acidsDifferent synthetasesSpecificity constant