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
1997
Glutaminyl-tRNA synthetase.
Freist W, Gauss D, Ibba M, Söll D. Glutaminyl-tRNA synthetase. Biological Chemistry 1997, 378: 1103-17. PMID: 9372179.Peer-Reviewed Original ResearchConceptsE. coli GlnRSGlutaminyl-tRNA synthetaseGlutamyl-tRNA synthetaseMammalian enzymeCommon ancestorPositive eubacteriaCognate tRNAMultienzyme complexTRNA moleculesGlnRArtificial mutantsAcceptor stemAnticodon loopMolecular massAmino acidsCatalytic siteEnzymeSynthetaseEubacteriaArchaebacteriaTRNAMutantsOrganellesAncestorComplexes
1993
Identification of a 100‐kDa protein associated with nuclear ribonuclease P activity in Schizosaccharomyces pombe
ZIMMERLY S, DRAINAS D, SYLVERS L, Dieter S. Identification of a 100‐kDa protein associated with nuclear ribonuclease P activity in Schizosaccharomyces pombe. The FEBS Journal 1993, 217: 501-507. PMID: 8223594, DOI: 10.1111/j.1432-1033.1993.tb18270.x.Peer-Reviewed Original ResearchConceptsFission yeast Schizosaccharomyces pombeYeast Schizosaccharomyces pombeGlycerol gradient fractionationCross-linking experimentsPrecursor tRNAsSchizosaccharomyces pombeRibonuclease PProtein interactsRNA componentProtein componentsP activityRibonuclease P activityApparent homogeneityDEAE-cellulose chromatographyPhosphocellulose chromatographySpecific fashionProtein
1979
Characterization of a UGA-suppressing serine tRNA from Schizosaccharomyces pombe with the help of a new in vitro assay system for eukaryotic suppressor tRNAs.
Kohli J, Kwong T, Altruda F, Söll D, Wahl G. Characterization of a UGA-suppressing serine tRNA from Schizosaccharomyces pombe with the help of a new in vitro assay system for eukaryotic suppressor tRNAs. Journal Of Biological Chemistry 1979, 254: 1546-1551. PMID: 762155, DOI: 10.1016/s0021-9258(17)37806-7.Peer-Reviewed Original ResearchConceptsOpal suppressor tRNASuppressor tRNAReadthrough productSchizosaccharomyces pombeFission yeast Schizosaccharomyces pombeYeast Schizosaccharomyces pombeOchre suppressor tRNAUGA termination codonBeta-globin mRNARabbit beta-globin mRNARabbit globin mRNAWheat germ extractSuppressor mutantsS. pombeNonsense suppressionPure tRNAsAlpha-globinSerine tRNATermination codonGlobin mRNATRNAPombeGerm extractSerineAssay systemThe nucleotide sequence of lysine tRNA 2 from Drosophila
Silverman S, Gillam I, Tener G, Söll D. The nucleotide sequence of lysine tRNA 2 from Drosophila. Nucleic Acids Research 1979, 6: 435-442. PMID: 106371, PMCID: PMC327705, DOI: 10.1093/nar/6.2.435.Peer-Reviewed Original Research
1972
Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli I. PURIFICATION AND PROPERTIES
Lapointe J, Söll D. Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli I. PURIFICATION AND PROPERTIES. Journal Of Biological Chemistry 1972, 247: 4966-4974. PMID: 4341531, DOI: 10.1016/s0021-9258(19)44925-9.Peer-Reviewed Original ResearchAdenosine TriphosphateAlkylationAmino AcidsAmino Acyl-tRNA SynthetasesAnimalsCatalysisCentrifugation, ZonalChromatographyDiphosphatesDrug StabilityElectrophoresisElectrophoresis, DiscEscherichia coliGlutamatesHot TemperatureHydroxyapatitesIsoelectric FocusingMacromolecular SubstancesMolecular WeightOxidation-ReductionPhosphorus IsotopesRabbitsUltracentrifugation
1967
An analysis of arginine codon multiplicity in rabbit hemoglobin
Weisblum B, Cherayil J, Bock R, Söll D. An analysis of arginine codon multiplicity in rabbit hemoglobin. Journal Of Molecular Biology 1967, 28: 275-280. PMID: 4861175, DOI: 10.1016/s0022-2836(67)80009-3.Peer-Reviewed Original Research