2000
Ancient Adaptation of the Active Site of Tryptophanyl-tRNA Synthetase for Tryptophan Binding †
Ibba M, Stange-Thomann N, Kitabatake M, Ali K, Söll I, Carter, C, Michael Ibba, and, Söll D. Ancient Adaptation of the Active Site of Tryptophanyl-tRNA Synthetase for Tryptophan Binding †. Biochemistry 2000, 39: 13136-13143. PMID: 11052665, DOI: 10.1021/bi001512t.Peer-Reviewed Original ResearchMeSH KeywordsAcylationAnimalsBacillus subtilisBacterial ProteinsBinding SitesCattleDiphosphatesDNA Mutational AnalysisDNA, BacterialEvolution, MolecularGeobacillus stearothermophilusHumansKineticsMiceMutagenesis, Site-DirectedProtein BindingRabbitsRNA, Transfer, TrpSequence Homology, Amino AcidTryptophanTryptophan-tRNA LigaseTyrosineConceptsAmino acid specificityActive site residuesTyrosyl-tRNA synthetasesTryptophanyl-tRNA synthetaseAncient adaptationAnalogous residuesGlu side chainsTryptophan replacementHomologous positionsSystematic mutationAromatic side chainsTrpRSTryptophan recognitionBacillus stearothermophilusSide chainsTryptophan bindingTyrRSResiduesCommon originCompetitive inhibitorMutationsTrp bindingMechanistic supportCatalytic efficiencyActive site
1998
Major Identity Element of Glutamine tRNAs from Bacillus subtilis and Escherichia coli in the Reaction with B. subtilis Glutamyl-tRNA Synthetase
Kim S, Söll D. Major Identity Element of Glutamine tRNAs from Bacillus subtilis and Escherichia coli in the Reaction with B. subtilis Glutamyl-tRNA Synthetase. Molecules And Cells 1998, 8: 459-465. PMID: 9749534, DOI: 10.1016/s1016-8478(23)13451-0.Peer-Reviewed Original Research
1997
Glu-tRNAGln amidotransferase: A novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation
Curnow A, Hong K, Yuan R, Kim S, Martins O, Winkler W, Henkin T, Söll D. Glu-tRNAGln amidotransferase: A novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 11819-11826. PMID: 9342321, PMCID: PMC23611, DOI: 10.1073/pnas.94.22.11819.Peer-Reviewed Original ResearchConceptsTranscriptional unitsGln-tRNAGlnGram-positive eubacteriaHeterotrimeric enzymeGlu-tRNAGlnTranslational apparatusHeterotrimeric proteinGlutamine codonB. subtilisAmidotransferaseSynthetase activityOnly pathwayEnzymeGlutamylEssential componentArchaeaTransamidationEubacteriaOperonCyanobacteriaGATCOrganellesCodonGenesGATAA nuclear genetic lesion affecting Saccharomyces cerevisiae mitochondrial translation is complemented by a homologous Bacillus gene
Kim S, Stange-Thomann N, Martins O, Hong K, Söll D, Fox T. A nuclear genetic lesion affecting Saccharomyces cerevisiae mitochondrial translation is complemented by a homologous Bacillus gene. Journal Of Bacteriology 1997, 179: 5625-5627. PMID: 9287027, PMCID: PMC179443, DOI: 10.1128/jb.179.17.5625-5627.1997.Peer-Reviewed Original ResearchMeSH KeywordsBacillus subtilisDNA, FungalDNA, MitochondrialFungal ProteinsGenes, BacterialMitochondrial ProteinsMolecular Sequence DataProtein BiosynthesisRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Analysis, DNASequence Homology, Amino AcidTransaminasesTranscription FactorstRNA-dependent amino acid transformations.
Curnow A, Hong K, Yuan R, Söll D. tRNA-dependent amino acid transformations. Nucleic Acids Symposium Series 1997, 2-4. PMID: 9478189.Peer-Reviewed Original ResearchMeSH KeywordsBacillus subtilisEscherichia coliModels, ChemicalNitrogenous Group TransferasesProtein Structure, TertiaryRNA, Bacterial
1996
Escherichia coli Tryptophanyl-tRNA Synthetase Mutants Selected for Tryptophan Auxotrophy Implicate the Dimer Interface in Optimizing Amino Acid Binding †
Sever S, Rogers K, Rogers M, Carter C, Söll D. Escherichia coli Tryptophanyl-tRNA Synthetase Mutants Selected for Tryptophan Auxotrophy Implicate the Dimer Interface in Optimizing Amino Acid Binding †. Biochemistry 1996, 35: 32-40. PMID: 8555191, DOI: 10.1021/bi952103d.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacillus subtilisBase SequenceBinding SitesCloning, MolecularDNA PrimersEscherichia coliGenes, BacterialGeobacillus stearothermophilusHaemophilus influenzaeKineticsMacromolecular SubstancesModels, MolecularMolecular Sequence DataPolymerase Chain ReactionProtein FoldingProtein Structure, SecondaryRecombinant ProteinsRestriction MappingSequence Homology, Amino AcidTryptophanTryptophan-tRNA LigaseConceptsTryptophanyl-tRNA synthetaseDimer interfaceClass I aminoacyl-tRNA synthetasesAminoacyl-tRNA synthetasesAmino acid bindingAmino acid activationActive siteSteady-state kinetic analysisSynthetase mutantsRossmann foldApparent KmKMSKS loopTrp lociProtein structureTrpR proteinTryptophan auxotrophDimeric enzymeAuxotrophic strainsBacillus stearothermophilusAcid bindingEscherichia coliOptimal catalysisAminoacyl adenylatesMutantsMutations
1989
delta-Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl-tRNA.
O'Neill G, Chen M, Söll D. delta-Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl-tRNA. FEMS Microbiology Letters 1989, 51: 255-9. PMID: 2511063, DOI: 10.1016/0378-1097(89)90406-0.Peer-Reviewed Original ResearchConceptsDelta-aminolevulinic acid biosynthesisChloroplasts of algaeTRNA-dependent transformationB. subtilisE. coliBacillus subtilisHigher plant speciesEscherichia coliPlant speciesAnaerobic eubacteriaGlutamyl-tRNAAcid biosynthesisCell-free extractsCell extractsBiosynthetic activitySubtilisDelta-aminolevulinic acidColiGabaculinAnaerobic conditionsAlaEubacteriaArchaebacteriaChloroplastsCyanobacteria