1973
Covalent attachment of fluorescent groups to the 5′-end of transfer RNA
Yang C, Söll D. Covalent attachment of fluorescent groups to the 5′-end of transfer RNA. Archives Of Biochemistry And Biophysics 1973, 155: 70-81. PMID: 4351348, DOI: 10.1016/s0003-9861(73)80010-4.Peer-Reviewed Original ResearchThe effect of growth temperatures on the in vivo ribose methylation of Bacillus stearothermophilus transfer RNA
Agris P, Koh H, Söll D. The effect of growth temperatures on the in vivo ribose methylation of Bacillus stearothermophilus transfer RNA. Archives Of Biochemistry And Biophysics 1973, 154: 277-282. PMID: 4689778, DOI: 10.1016/0003-9861(73)90058-1.Peer-Reviewed Original Research
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 inactivationInactivationLeuGluProperties of a dimer of tRNA I Tyr 1 (Escherichia coli).
Yang S, Söll D, Crothers D. Properties of a dimer of tRNA I Tyr 1 (Escherichia coli). Biochemistry 1972, 11: 2311-20. PMID: 4555033, DOI: 10.1021/bi00762a016.Peer-Reviewed Original ResearchAmino Acyl-tRNA SynthetasesCarbon IsotopesChemical PhenomenaChemistryChemistry, PhysicalEscherichia coliHot TemperatureKineticsMacromolecular SubstancesMagnesiumMathematicsModels, ChemicalModels, StructuralNucleic Acid ConformationNucleic Acid DenaturationNucleic Acid HybridizationRNA, BacterialRNA, TransferSodiumSpectrophotometryTemperatureThermodynamicsTyrosineUltracentrifugationUltraviolet Rays
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, GeneticTobaccoValine
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 extractBiosynthesisGenesPolymerasePseudouridineSpColiResiduesIsolation and properties of a transfer ribonucleic acid deficient in ribothymidine.
Johnson L, Hayashi H, Soell D. Isolation and properties of a transfer ribonucleic acid deficient in ribothymidine. Biochemistry 1970, 9: 2823-31. PMID: 4918123, DOI: 10.1021/bi00816a011.Peer-Reviewed Original ResearchPurification of Five Serine Transfer Ribonucleic Acid Species from Escherichia coli and Their Acylation by Homologous and Heterologous Seryl Transfer Ribonucleic Acid Synthetases
Roy K, Söll D. Purification of Five Serine Transfer Ribonucleic Acid Species from Escherichia coli and Their Acylation by Homologous and Heterologous Seryl Transfer Ribonucleic Acid Synthetases. Journal Of Biological Chemistry 1970, 245: 1394-1400. PMID: 4910052, DOI: 10.1016/s0021-9258(18)63249-1.Peer-Reviewed Original Research
1969
Transfer ribonucleic acid from Mycoplasma.
Hayashi H, Fisher H, Soell D. Transfer ribonucleic acid from Mycoplasma. Biochemistry 1969, 8: 3680-6. PMID: 4897946, DOI: 10.1021/bi00837a028.Peer-Reviewed Original ResearchAmino AcidsCarbon IsotopesCell-Free SystemCelluloseChemical PhenomenaChemistryChromatography, Ion ExchangeChromatography, PaperElectrophoresisEscherichia coliFormatesHot TemperatureMethionineMycoplasmaNucleic Acid DenaturationNucleosidesPeptide BiosynthesisPolynucleotidesRNA, BacterialRNA, TransferSpecies SpecificityStimulation, ChemicalTritiumUltracentrifugationUracil Nucleotides
1968
Structure and function of Escherichia coli ribosomes II. Translational fidelity and efficiency in protein synthesis of a protein-deficient subribosomal particle
Traub P, Söll D, Nomura M. Structure and function of Escherichia coli ribosomes II. Translational fidelity and efficiency in protein synthesis of a protein-deficient subribosomal particle. Journal Of Molecular Biology 1968, 34: 595-608. PMID: 4938559, DOI: 10.1016/0022-2836(68)90183-6.Peer-Reviewed Original ResearchStudies on polynucleotides LXXXV. Partial purification of an amber supressor tRNA and studies on in vitro suppression
Söll D. Studies on polynucleotides LXXXV. Partial purification of an amber supressor tRNA and studies on in vitro suppression. Journal Of Molecular Biology 1968, 34: 175-187. PMID: 4938541, DOI: 10.1016/0022-2836(68)90243-x.Peer-Reviewed Original ResearchConceptsSuppressor tRNAColi cellsAmber suppressor genesAmber suppressor tRNAProtein synthesis experimentsEscherichia coli cellsE. coli cellsAmber mutantsTRNASuppressor geneProtein synthesisCrude tRNAGenesRNAPartial purificationBacteriophage f2CellsMutantsRibosomesUAGSpeciesMessengerSuppressionChain terminationBindingBiosynthesis of the Peptidoglycan of Bacterial Cell Walls X. Further Study of the Glycyl Transfer Ribonucleic Acids Active in Peptidoglycan Synthesis in Staphylococcus Aureus
Bumsted R, Dahl J, Söll D, Strominger J. Biosynthesis of the Peptidoglycan of Bacterial Cell Walls X. Further Study of the Glycyl Transfer Ribonucleic Acids Active in Peptidoglycan Synthesis in Staphylococcus Aureus. Journal Of Biological Chemistry 1968, 243: 779-782. PMID: 4867040, DOI: 10.1016/s0021-9258(19)81733-7.Peer-Reviewed Original ResearchBiosynthesis of the Peptidoglycan of Bacterial Cell Walls VI. Incorporation Of l-Threonine Into Interpeptide Bridges in Micrococcus Roseus
Roberts W, Strominger J, Söll D. Biosynthesis of the Peptidoglycan of Bacterial Cell Walls VI. Incorporation Of l-Threonine Into Interpeptide Bridges in Micrococcus Roseus. Journal Of Biological Chemistry 1968, 243: 749-756. PMID: 5638591, DOI: 10.1016/s0021-9258(19)81729-5.Peer-Reviewed Original ResearchBiosynthesis of the Peptidoglycan of Bacterial Cell Walls VII. Incorporation of Serine and Glycine into Interpeptide Bridges in Staphylococcus Epidermidis
Petit J, Strominger J, Söll D. Biosynthesis of the Peptidoglycan of Bacterial Cell Walls VII. Incorporation of Serine and Glycine into Interpeptide Bridges in Staphylococcus Epidermidis. Journal Of Biological Chemistry 1968, 243: 757-767. PMID: 5638592, DOI: 10.1016/s0021-9258(19)81730-1.Peer-Reviewed Original ResearchMeSH KeywordsAlcoholsBacitracinCarbon IsotopesCell WallChloramphenicolChlortetracyclineChromatography, Ion ExchangeCycloserineErythromycinGlycoproteinsLincomycinNovobiocinPenicillinsPeptide BiosynthesisPolysaccharides, BacterialPuromycinRistocetinSerineStaphylococcusStreptomycinSurface-Active AgentsTritiumVancomycinConceptsPeptidoglycan synthesis
1967
Studies on polynucleotides LXXVI. Specificity of transfer RNA for codon recognition as studied by amino acid incorporation
Söll D, RajBhandary U. Studies on polynucleotides LXXVI. Specificity of transfer RNA for codon recognition as studied by amino acid incorporation. Journal Of Molecular Biology 1967, 29: 113-124. PMID: 4861608, DOI: 10.1016/0022-2836(67)90184-2.Peer-Reviewed Original ResearchStudies on polynucleotides LXXV. Specificity of tRNA for codon recognition as studied by the ribosomal binding technique
Söll D, Cherayil J, Bock R. Studies on polynucleotides LXXV. Specificity of tRNA for codon recognition as studied by the ribosomal binding technique. Journal Of Molecular Biology 1967, 29: 97-112. PMID: 4861614, DOI: 10.1016/0022-2836(67)90183-0.Peer-Reviewed Original ResearchConceptsTransfer RNAAmino acidsE. coliIndividual amino acidsCodon recognitionMultiple codonsMultiple speciesRespective amino acidsWobble hypothesisYeast transfer RNAEscherichia coliCodonRNAColiYeastSpeciesBindingRecognition patternsTRNARibosomesThird letterStimulation of bindingTrinucleotideAcidInteresting differencesAn 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