2000
Methanococcus jannaschii Prolyl-Cysteinyl-tRNA Synthetase Possesses Overlapping Amino Acid Binding Sites †
Stathopoulos C, Jacquin-Becker C, Becker H, Li T, Ambrogelly A, Longman R, Söll D. Methanococcus jannaschii Prolyl-Cysteinyl-tRNA Synthetase Possesses Overlapping Amino Acid Binding Sites †. Biochemistry 2000, 40: 46-52. PMID: 11141055, DOI: 10.1021/bi002108x.Peer-Reviewed Original ResearchConceptsAmino acidsTRNA synthetaseProtein translation apparatusCysteinyl-tRNA synthetase activityCognate tRNA speciesSite-directed mutagenesisAmino acid activationAbsence of tRNAAmino acid residuesSynthetase activityTranslation apparatusMethanococcus jannaschiiTRNA speciesCysteine activationUnusual enzymeDifferent amino acidsMutant enzymesCysteine bindingProline bindingProlyl-tRNA synthetase activityAcid residuesAminoacyl-tRNAPosition 103Single enzymeTransfer RNA Identity Change in Anticodon Variants of E. coli tRNAPhe in Vivo
Kim H, Kim I, Söll D, Lee Y. Transfer RNA Identity Change in Anticodon Variants of E. coli tRNAPhe in Vivo. Molecules And Cells 2000, 10: 76-82. PMID: 10774751, DOI: 10.1007/s10059-000-0076-7.Peer-Reviewed Original ResearchConceptsMutant tRNA genesMutant tRNAsTRNA genesAnticodon sequenceAnticodon mutantsHost viabilityE. coliAmino acidsMost aminoacyl-tRNA synthetasesOpal stop codonAminoacyl-tRNA synthetasesSite-directed mutagenesisE. coli tRNAMajor recognition elementAnticodon variantsSuch tRNAsTRNAStop codonAminoacylation specificityAnticodonSimilarity dendrogramVivo evolutionGenesAcceptor specificityAnticodon change
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
1988
Site-directed mutagenesis to fine-tune enzyme specificity
Uemura H, Rogers M, Swanson R, Watson L, Söll D. Site-directed mutagenesis to fine-tune enzyme specificity. Protein Engineering Design And Selection 1988, 2: 293-296. PMID: 3150543, DOI: 10.1093/protein/2.4.293.Peer-Reviewed Original ResearchConceptsOligonucleotide-directed mutagenesisEscherichia coli glutaminyl-tRNA synthetaseGenetic selectionGlutaminyl-tRNA synthetaseAmino acid replacementsSite-directed mutagenesisAcid replacementsEnzyme specificitySingle residueMutagenesisSide chainsRepulsive charge-charge interactionsSpecific recognitionCharge-charge interactionsNucleic acidsMutantsProteinSupFSynthetaseResiduesGlutamineSelection