2012
Yeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignment
Ling J, Peterson KM, Simonović I, Cho C, Söll D, Simonović M. Yeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignment. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 3281-3286. PMID: 22343532, PMCID: PMC3295322, DOI: 10.1073/pnas.1200109109.Peer-Reviewed Original ResearchMeSH KeywordsAeropyrumAmino Acid SequenceAnticodonCatalytic DomainCodonCrystallography, X-RayEscherichia coliEvolution, MolecularLeucineMitochondriaModels, MolecularMolecular Sequence DataProtein ConformationProtein Structure, TertiaryRNA EditingRNA, Transfer, Amino AcylSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSpecies SpecificityStaphylococcus aureusSubstrate SpecificityThreonineThreonine-tRNA LigaseConceptsThreonyl-tRNA synthetaseAnticodon loopAnticodon sequenceEscherichia coli ThrRSSet of tRNAsDistinct recognition mechanismsAnticodon-binding domainAminoacyl-tRNA synthetasesCUN codonsDetailed structural comparisonCodon reassignmentYeast mitochondriaGenetic codeTRNA isoacceptorsSaccharomyces cerevisiaeIsoacceptor tRNAsEditing domainTRNAMST1Anticodon tripletStructural comparisonNatural tRNAAmino acidsDistinct mechanismsRecognition mechanism
1994
A Lactobacillus nifS-like gene suppresses an Escherichia coli transaminase B mutation
Leong-Morgenthaler P, Oliver S, Hottinger H, Söll D. A Lactobacillus nifS-like gene suppresses an Escherichia coli transaminase B mutation. Biochimie 1994, 76: 45-49. PMID: 8031904, DOI: 10.1016/0300-9084(94)90061-2.Peer-Reviewed Original ResearchConceptsNifS-like genesNifS-like proteinsNif gene productsNif proteinsNif genesGene productsNitrogen-fixing bacteriaGroup of enzymesRemarkable sequence homologyCysteine desulfuraseSequence conservationEfficient nitrogen fixationLeucine auxotrophyTransaminase BDiverse functionsSequence homologyNitrogen fixationEscherichia coli strainsProtein productsMetabolic pathwaysAzotobacter vinelandiiGenesB mutationsProteinDissimilar mutations
1987
Allele-specific complementation of an Escherichia coli leuB mutation by a Lactobacillus bulgaricus tRNA gene
Hottinger H, Ohgi T, Zwahlen M, Dhamija S, Söll D. Allele-specific complementation of an Escherichia coli leuB mutation by a Lactobacillus bulgaricus tRNA gene. Gene 1987, 60: 75-83. PMID: 3326787, DOI: 10.1016/0378-1119(87)90215-0.Peer-Reviewed Original ResearchConceptsTRNA genesCopy numberWild-type formE. coli promotersHigh copy numberGene copy numberLeuB mutationClone bankLeucine prototrophyLow copy numberMissense suppressionNucleotide sequenceSerine tRNATerminator elementsGenesRestoration of activityTRNAEscherichia coliAmino acidsGene allelesExtra armE. coli
1984
The sup8 tRNALeu gene of Schizosaccharomyces pombe has an unusual intervening sequence and reduced pairing in the anticodon stem
Sumner-Smith M, Hottinger H, Willis I, Koch T, Arentzen R, Söll D. The sup8 tRNALeu gene of Schizosaccharomyces pombe has an unusual intervening sequence and reduced pairing in the anticodon stem. Molecular Genetics And Genomics 1984, 197: 447-452. PMID: 6597338, DOI: 10.1007/bf00329941.Peer-Reviewed Original ResearchConceptsTRNA genesS. pombe DNAWild-type alleleAnticodon UCASplicing endonucleaseSuppressor allelesSchizosaccharomyces pombeTRNALeu geneUUA codonTrailer sequencesIntervening sequenceCell-free extractsAnticodon stemRelated sequencesSplice siteBase pairsSecondary structureGenesIsoacceptorsAllelesSequenceStructural requirementsPombeAnticodonSup8
1977
Regulation of biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coli II. Isolation of regulatory mutants affecting leucyl-tRNA synthetase levels
LaRossa R, Vögeli G, Low K, Söll D. Regulation of biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coli II. Isolation of regulatory mutants affecting leucyl-tRNA synthetase levels. Journal Of Molecular Biology 1977, 117: 1033-1048. PMID: 342703, DOI: 10.1016/s0022-2836(77)80011-9.Peer-Reviewed Original ResearchConceptsLeucyl-tRNA synthetaseThermolabile leucyl-tRNA synthetaseRegulation of biosynthesisDistinct genetic lociAminoacyl-tRNA synthetasesEscherichia coli IIOperator-promoter regionStructural geneRegulatory mutantsGenetic lociEscherichia coli strainsSuch revertantsSpontaneous revertantsThermolabile enzymeLociSynthetaseColi strainsRevertantsSynthetase levelsLeuTRNAMutantsSynthetasesLeuXBiosynthesisRegulation of biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coli III. Biochemical characterization of regulatory mutants affecting leucyl-tRNA synthetase levels
LaRossa R, Mao J, Low K, Söll D. Regulation of biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coli III. Biochemical characterization of regulatory mutants affecting leucyl-tRNA synthetase levels. Journal Of Molecular Biology 1977, 117: 1049-1059. PMID: 342704, DOI: 10.1016/s0022-2836(77)80012-0.Peer-Reviewed Original ResearchConceptsAminoacyl-tRNA synthetasesLeucyl-tRNA synthetaseProtein synthesisRegulation of biosynthesisEscherichia coli IIIIsoacceptor familiesIlv operonRegulatory mutantsSteady-state levelsAmount of tRNALeu operonBiochemical characterizationCellular concentrationSynthetasesEscherichia coliOperonControl elementsTRNASynthetaseSynthetase levelsMutationsDerepressionPpGppMutantsPppGpp
1972
Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli II. INTERACTION WITH INTACT GLUTAMYL TRANSFER RIBONUCLEIC ACID
Lapointe J, Söll D. Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli II. INTERACTION WITH INTACT GLUTAMYL TRANSFER RIBONUCLEIC ACID. Journal Of Biological Chemistry 1972, 247: 4975-4981. PMID: 4341532, DOI: 10.1016/s0021-9258(19)44926-0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acyl-tRNA SynthetasesCarbon IsotopesCatalysisCentrifugation, Density GradientDiphosphatesDrug StabilityEscherichia coliGlutamatesHot TemperatureHydrogen-Ion ConcentrationKineticsLeucineMagnesiumPhosphorus IsotopesProtein BindingRNA, TransferSpectrometry, FluorescenceValineConceptsGlutamyl-transfer ribonucleic acid synthetaseEscherichia coli IITransfer ribonucleic acidTRNA-GluTRNA-ValTRNA-LeuCognate tRNABiological specificityRibonucleic acidPure enzymeEnzymeSimilar Km valuesComplex formationGradient centrifugationSynthetaseKm valuesFluorescence-quenching studiesTRNAIsoacceptorsComplexesFluorescence quenching studiesHeat inactivationInactivationLeuGluInvestigation of adenovirus-directed 4S RNA
Kline L, Weissman S, Söll D. Investigation of adenovirus-directed 4S RNA. Virology 1972, 48: 291-296. PMID: 5017153, DOI: 10.1016/0042-6822(72)90142-0.Peer-Reviewed Original Research
1971
Isolation and Partial Characterization of Temperature-Sensitive Escherichia coli Mutants with Altered Leucyl- and Seryl-Transfer Ribonucleic Acid Synthetases
Low B, Gates F, Goldstein T, Söll D. Isolation and Partial Characterization of Temperature-Sensitive Escherichia coli Mutants with Altered Leucyl- and Seryl-Transfer Ribonucleic Acid Synthetases. Journal Of Bacteriology 1971, 108: 742-750. PMID: 4942762, PMCID: PMC247134, DOI: 10.1128/jb.108.2.742-750.1971.Peer-Reviewed Original ResearchConceptsLeucyl-tRNA synthetaseTemperature-sensitive Escherichia coli mutantsCorresponding genetic lociEscherichia coli mutantsSeryl-tRNA synthetaseTemperature-sensitive mutantColi mutantsGenetic lociBranched-chain amino acidsEscherichia coliAmino acidsConditional growthSynthetaseMutantsPartial characterizationEnzymePurification of Five Leucine Transfer Ribonucleic Acid Species from Escherichia coli and Their Acylation by Heterologous Leucyl-Transfer Ribonucleic Acid Synthetase
Blank H, Söll D. Purification of Five Leucine Transfer Ribonucleic Acid Species from Escherichia coli and Their Acylation by Heterologous Leucyl-Transfer Ribonucleic Acid Synthetase. Journal Of Biological Chemistry 1971, 246: 4947-4950. PMID: 4936719, DOI: 10.1016/s0021-9258(18)61954-4.Peer-Reviewed Original ResearchMeSH KeywordsAcylationBase SequenceBenzoatesCarbon IsotopesCarcinomaCell LineChromatography, DEAE-CelluloseChromatography, GelDrug StabilityEscherichia coliGenetic CodeHot TemperatureKineticsLeucineLigasesMouth NeoplasmsNucleic Acid DenaturationPolynucleotidesRibosomesRNA, BacterialRNA, TransferTemplates, GeneticYeastsA Comparative Study of the Interactions of Escherichia coli Leucyl-, Seryl-, and Valyl-Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic Acids
Myers G, Blank H, Söll D. A Comparative Study of the Interactions of Escherichia coli Leucyl-, Seryl-, and Valyl-Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic Acids. Journal Of Biological Chemistry 1971, 246: 4955-4964. PMID: 4936720, DOI: 10.1016/s0021-9258(18)61956-8.Peer-Reviewed Original ResearchConceptsEscherichia coli KSeryl-tRNA synthetaseLeucyl-tRNA synthetaseRibonucleic acidTransfer ribonucleic acidValyl-tRNA synthetaseTRNA recognitionColi KSynthetase-tRNA complexIsoacceptorsAmino acidsEquilibrium binding studiesPing-pong typeTRNASynthetaseEnzymeKm valuesSubstrate inhibitionBasic similaritiesBinding studiesSerylAcidATPSame bufferSequencePurification of an Escherichia coli Leucine Suppressor Transfer Ribonucleic Acid and Its Aminoacylation by the Homologous Leucyl-Transfer Ribonucleic Acid Synthetase
Hayashi H, Söll D. Purification of an Escherichia coli Leucine Suppressor Transfer Ribonucleic Acid and Its Aminoacylation by the Homologous Leucyl-Transfer Ribonucleic Acid Synthetase. Journal Of Biological Chemistry 1971, 246: 4951-4954. PMID: 4941862, DOI: 10.1016/s0021-9258(18)61955-6.Peer-Reviewed Original ResearchMeSH KeywordsAcylationBenzoatesBiological AssayCarbon IsotopesChromatography, DEAE-CelluloseColiphagesEscherichia coliGenetics, MicrobialKineticsLeucineLigasesMutationPeptide BiosynthesisPlant Growth RegulatorsPlants, ToxicPolynucleotidesRNA, TransferSuppression, GeneticTemplates, GeneticTobaccoValineThe nucleotide sequence of two leucine tRNA species from Escherichia coli K12
Blank H, Sőll D. The nucleotide sequence of two leucine tRNA species from Escherichia coli K12. Biochemical And Biophysical Research Communications 1971, 43: 1192-1197. PMID: 4936129, DOI: 10.1016/0006-291x(71)90589-4.Peer-Reviewed Original Research
1970
Purification of Leucyl Transfer Ribonucleic Acid Synthetase from Escherichia coli
Hayashi H, Knowles J, Katze J, Lapointe J, Söll D. Purification of Leucyl Transfer Ribonucleic Acid Synthetase from Escherichia coli. Journal Of Biological Chemistry 1970, 245: 1401-1406. PMID: 4986473, DOI: 10.1016/s0021-9258(18)63250-8.Peer-Reviewed Original ResearchMeSH KeywordsAlkylationAmino AcidsChromatographyChromatography, DEAE-CelluloseDrug StabilityEdetic AcidElectrophoresisEscherichia coliHydrogen-Ion ConcentrationHydroxyapatitesLeucineLigasesMethodsMolecular WeightOxidation-ReductionRNA, BacterialRNA, TransferSodium ChlorideTemperatureTime FactorsUltracentrifugationThe Interaction of Seryl and of Leucyl Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic Acids
Knowles J, Katze J, Konigsberg W, Söll D. The Interaction of Seryl and of Leucyl Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic Acids. Journal Of Biological Chemistry 1970, 245: 1407-1415. PMID: 4910800, DOI: 10.1016/s0021-9258(18)63251-x.Peer-Reviewed Original ResearchConceptsSeryl-tRNA synthetaseTransfer ribonucleic acidComplex formationTransfer RNA speciesLeucyl-tRNA synthetaseRibonucleic acidRNA speciesCognate tRNAEscherichia coliSynthetaseDensity gradient centrifugationTRNAStable complexesHigh saltGradient centrifugationSpeciesGel filtrationComplexesSerylColiATPEnzymeAcidSerFormation
1966
sRNA specificity for codon recognition as studied by the ribosomal binding technique.
Söll D, Cherayil J, Jones D, Faulkner R, Hapel A, Bock R, Khorana H. sRNA specificity for codon recognition as studied by the ribosomal binding technique. Cold Spring Harbor Symposia On Quantitative Biology 1966, 31: 51-61. PMID: 4866399, DOI: 10.1101/sqb.1966.031.01.011.Peer-Reviewed Original Research