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
Glutamyl-tRNAGln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis
Curnow A, Tumbula D, Pelaschier J, Min B, Söll D. Glutamyl-tRNAGln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 12838-12843. PMID: 9789001, PMCID: PMC23620, DOI: 10.1073/pnas.95.22.12838.Peer-Reviewed Original ResearchConceptsDeinococcus radioduransD. radiodurans genomeRadiation-resistant bacterium Deinococcus radioduransBiosynthesis of asparagineGlutaminyl-tRNA synthetaseGlutamyl-tRNA synthetaseBacterium Deinococcus radioduransPresence of AsnRSAsparaginyl-tRNA synthetaseAspartyl-tRNA synthetaseAsn-tRNAAsparagine biosynthesisAsparaginyl-tRNAGenomic sequencesGln-tRNAAsparagine synthetaseBiochemical experimentsTransamidation activityGlutaminyl-tRNAProtein synthesisSingle enzymeSynthetaseRadioduransBiosynthesisGenes
1991
delta-Aminolevulinic acid dehydratase deficiency can cause delta-aminolevulinate auxotrophy in Escherichia coli
O'Neill G, Thorbjarnardóttir S, Michelsen U, Pálsson S, Söll D, Eggertsson G. delta-Aminolevulinic acid dehydratase deficiency can cause delta-aminolevulinate auxotrophy in Escherichia coli. Journal Of Bacteriology 1991, 173: 94-100. PMID: 1987138, PMCID: PMC207161, DOI: 10.1128/jb.173.1.94-100.1991.Peer-Reviewed Original ResearchConceptsALA dehydratase activityEscherichia coliWild-type geneClasses of mutantsDNA sequence analysisAminoglycoside antibiotic kanamycinHeme biosynthetic pathwayALA biosynthesisWild-type DNAAuxotrophic phenotypeComplementation studiesDehydratase activityHemB geneBiosynthetic pathwayPositive regulationALA formationSame geneMutantsPenicillin enrichmentSequence analysisGenesAntibiotic kanamycinDiffusible productHemB mutantEnzymatic activity
1989
Characterization of cis-acting mutations which increase expression of a glnS-lacZ fusion in Escherichia coli
Plumbridge J, Söll D. Characterization of cis-acting mutations which increase expression of a glnS-lacZ fusion in Escherichia coli. Molecular Genetics And Genomics 1989, 216: 113-119. PMID: 2471922, DOI: 10.1007/bf00332238.Peer-Reviewed Original Research
1988
Escherichia coli glutaminyl-tRNA synthetase: a single amino acid replacement relaxes rRNA specificity.
Uemura H, Conley J, Yamao F, Rogers J, Söll D. Escherichia coli glutaminyl-tRNA synthetase: a single amino acid replacement relaxes rRNA specificity. Protein Sequences And Data Analysis 1988, 1: 479-85. PMID: 2464170.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseTRNA bindingEscherichia coli glutaminyl-tRNA synthetaseExtensive homology searchesSingle amino acid replacementSingle amino acid changeRegion of homologyAminoacyl-tRNA synthetasesAmino acid replacementsAminoacyl adenylate formationAmino acids 235Amino acid changesLittle apparent similarityGlnS geneTRNA discriminationHomology searchGene productsAcid replacementsShare regionsDifferent tRNAsShort stretchesGenetic selectionAcid changesAsn changeHomology
1987
The effect of dam methylation on the expression of glnS in E. coli
Plumbridge J, Söll D. The effect of dam methylation on the expression of glnS in E. coli. Biochimie 1987, 69: 539-541. PMID: 2960382, DOI: 10.1016/0300-9084(87)90091-5.Peer-Reviewed Original Research
1984
In vivo and in vitro transcription of the Escherichia coli glutaminyl-tRNA synthetase gene.
Cheung A, Söll D. In vivo and in vitro transcription of the Escherichia coli glutaminyl-tRNA synthetase gene. Journal Of Biological Chemistry 1984, 259: 9953-9958. PMID: 6086662, DOI: 10.1016/s0021-9258(17)42791-8.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseGlutaminyl-tRNA synthetase geneTranslation initiation codon AUGInitiation codon AUGPresence of tRNATermination codon UAAGlnS geneTerminator structureTranscription initiationSynthetase geneTranscription initiatesCodons UAARegulatory signalsCodon AUGTermination sitesTranscription productsSequence analysisStructure upstreamStructural regionsTranscriptionGenesTranscriptsSynthetaseMRNAGln
1982
Escherichia coli glutaminyl-tRNA synthetase. I. Isolation and DNA sequence of the glnS gene.
Yamao F, Inokuchi H, Cheung A, Ozeki H, Söll D. Escherichia coli glutaminyl-tRNA synthetase. I. Isolation and DNA sequence of the glnS gene. Journal Of Biological Chemistry 1982, 257: 11639-11643. PMID: 6288695, DOI: 10.1016/s0021-9258(18)33810-9.Peer-Reviewed Original ResearchEscherichia coli glutaminyl-tRNA synthetase. II. Characterization of the glnS gene product.
Hoben P, Royal N, Cheung A, Yamao F, Biemann K, Söll D. Escherichia coli glutaminyl-tRNA synthetase. II. Characterization of the glnS gene product. Journal Of Biological Chemistry 1982, 257: 11644-11650. PMID: 6749844, DOI: 10.1016/s0021-9258(18)33811-0.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetasePrimary sequenceDNA sequencesAminoacyl-tRNA synthetasesManual Edman degradationExtensive sequence repeatsCarboxypeptidase B digestionEscherichia coli K12NH2-terminal sequenceSequence repeatsStructural geneGene productsCarboxyl terminusSequence homologyHomologous regionsTwo-column procedureEdman degradationColi K12B digestionSynthetaseSynthetasesTheoretical peptidesSequencePosition 550Enzyme
1970
In Vitro Biosynthesis of Pseudouridine at the Polynucleotide Level by an Enzyme Extract from Escherichia coli
Johnson L, Söll D. In Vitro Biosynthesis of Pseudouridine at the Polynucleotide Level by an Enzyme Extract from Escherichia coli. Proceedings Of The National Academy Of Sciences Of The United States Of America 1970, 67: 943-950. PMID: 4943184, PMCID: PMC283296, DOI: 10.1073/pnas.67.2.943.Peer-Reviewed Original ResearchConceptsE. coli RNA polymeraseRNA transcription productsColi RNA polymeraseConversion of uridineE. coli extractsTRNA genesRNA polymerasePolynucleotide levelUridine residuesTranscription productsVitro BiosynthesisMycoplasma spEscherichia coliLambda DNARNADNAMacromolecular levelEnzyme extractBiosynthesisGenesPolymerasePseudouridineSpColiResidues