1991
Purification and functional characterization of glutamate-1-semialdehyde aminotransferase from Chlamydomonas reinhardtii.
Jahn D, Chen M, Söll D. Purification and functional characterization of glutamate-1-semialdehyde aminotransferase from Chlamydomonas reinhardtii. Journal Of Biological Chemistry 1991, 266: 161-167. PMID: 1985889, DOI: 10.1016/s0021-9258(18)52416-9.Peer-Reviewed Original ResearchMeSH KeywordsAminooxyacetic AcidCell MembraneChlamydomonasChromatography, DEAE-CelluloseChromatography, GelChromatography, High Pressure LiquidChromatography, Ion ExchangeCyclohexanecarboxylic AcidsElectrophoresis, Polyacrylamide GelIntramolecular TransferasesIsomerasesKineticsMolecular WeightPyridoxal PhosphateConceptsGlutamate-1-semialdehyde aminotransferaseGlutamyl-tRNA synthetaseC5 pathwayChlamydomonas reinhardtiiGreen alga Chlamydomonas reinhardtiiGlu-tRNA reductaseTRNA-dependent transformationChloroplasts of plantsGlutamyl-tRNA reductaseAlga Chlamydomonas reinhardtiiDelta-aminolevulinic acidApparent molecular massWhole cell extractsChlorophyll biosynthesisSodium dodecyl sulfate-polyacrylamide gel electrophoresisC. reinhardtiiDodecyl sulfate-polyacrylamide gel electrophoresisSulfate-polyacrylamide gel electrophoresisRate zonal sedimentationFunctional characterizationThird enzymeGlycerol gradientsCell extractsReinhardtiiMembrane fraction
1990
Purification and characterization of Chlamydomonas reinhardtii chloroplast glutamyl-tRNA synthetase, a natural misacylating enzyme.
Chen M, Jahn D, Schön A, O'Neill G, Söll D. Purification and characterization of Chlamydomonas reinhardtii chloroplast glutamyl-tRNA synthetase, a natural misacylating enzyme. Journal Of Biological Chemistry 1990, 265: 4054-4057. PMID: 2303494, DOI: 10.1016/s0021-9258(19)39701-7.Peer-Reviewed Original ResearchConceptsGlutamyl-tRNA synthetaseChloroplast enzymeApparent molecular massSequential column chromatographyChlamydomonas reinhardtiiActive enzymeMolecular massNondenaturing conditionsEscherichia coliDenaturing conditionsAcceptor RNASynthetaseMono S.Mono QEnzymeTRNAReinhardtiiYeastColumn chromatographyRNACytoplasmicProteinBarleyColiReversed phase chromatographyPurification of the glutamyl-tRNA reductase from Chlamydomonas reinhardtii involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis.
Chen M, Jahn D, O'Neill G, Söll D. Purification of the glutamyl-tRNA reductase from Chlamydomonas reinhardtii involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis. Journal Of Biological Chemistry 1990, 265: 4058-4063. PMID: 2303495, DOI: 10.1016/s0021-9258(19)39702-9.Peer-Reviewed Original ResearchConceptsGlu-tRNA reductaseGlutamyl-tRNA reductaseGlu-tRNAChlamydomonas reinhardtiiTRNA-dependent transformationChloroplasts of plantsDelta-aminolevulinic acid formationApparent molecular massChlorophyll biosynthesisGlutamyl-tRNAHomologous tRNAsSecond enzymeActive enzymeMolecular massNondenaturing conditionsDifferent chromatographic separationsCertain bacteriaReductaseDelta-aminolevulinic acidReinhardtiiPorphyrin biosynthesisBiosynthesisStable complexesChromatographic separationCarboxyl groupsEnzymatic addition of guanylate to histidine transfer RNA
Williams J, Cooley L, Söll D. Enzymatic addition of guanylate to histidine transfer RNA. Methods In Enzymology 1990, 181: 451-462. PMID: 2166216, DOI: 10.1016/0076-6879(90)81143-i.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineChromatography, AffinityChromatography, DEAE-CelluloseChromatography, Ion ExchangeDrosophilaElectrophoresis, Polyacrylamide GelGuanosine TriphosphateKineticsNucleotidyltransferasesPhosphorus RadioisotopesRadioisotope Dilution TechniqueRNA, Transfer, Amino Acid-SpecificRNA, Transfer, HisSaccharomyces cerevisiaeSubstrate SpecificityConceptsHistidine tRNATransfer RNABacteriophage T5Yeast enzymeEnzyme migratesUridine residuesExtra nucleotidesLigase mechanismAdditional nucleotidesEnzymatic additionGel filtration chromatographyEnzyme intermediateTRNAAbsolute requirementEnzymeMolecular weightNucleotidesUltrogel AcA 34Filtration chromatographyATPDrosophilaAcA 34Molecular weight markersYeastTitration experiments
1985
[8] Glutaminyl-tRNA synthetase of Escherichia coli
Hoben P, Söll D. [8] Glutaminyl-tRNA synthetase of Escherichia coli. Methods In Enzymology 1985, 113: 55-59. PMID: 3911010, DOI: 10.1016/s0076-6879(85)13011-9.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesCarbon RadioisotopesChromatography, DEAE-CelluloseChromatography, Ion ExchangeEscherichia coliKineticsRadioisotope Dilution TechniqueConceptsGlutaminyl-tRNA synthetaseStructural geneSpecific aminoacyl-tRNA synthetaseE. coli chromosomeAmino acidsCognate amino acidTemperature-sensitive phenotypeGlutamyl-tRNA synthetaseAminoacyl-tRNA synthetaseColi chromosomeGln-tRNAGlnDNA fragmentsProtein synthesisEscherichia coliThermolabile enzymeCellular levelGenesGln mutationSynthetaseGlnRE. coliSeparate enzymesMultistep processNegative bacteriaEnzyme
1974
N‐(purin‐6‐ylcarbamoyl)threonine: Biosynthesis in vitro in transfer RNA by an enzyme purified from Escherichia coli
Körner A, Söll D. N‐(purin‐6‐ylcarbamoyl)threonine: Biosynthesis in vitro in transfer RNA by an enzyme purified from Escherichia coli. FEBS Letters 1974, 39: 301-306. PMID: 4604806, DOI: 10.1016/0014-5793(74)80135-3.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseAmino Acyl-tRNA SynthetasesCarbamatesCarbon RadioisotopesChromatography, DEAE-CelluloseChromatography, Ion ExchangeChromatography, PaperChromatography, Thin LayerElectrophoresis, PaperEscherichia coliIsotope LabelingMutationNitrosoguanidinesPhosphorus RadioisotopesPurine NucleosidesRibonucleasesRNA, BacterialRNA, TransferSpectrophotometry, UltravioletThreonineTime FactorsTritium
1972
Is There a Discriminator Site in Transfer RNA?
Crothers D, Seno T, Söll D. Is There a Discriminator Site in Transfer RNA? Proceedings Of The National Academy Of Sciences Of The United States Of America 1972, 69: 3063-3067. PMID: 4562753, PMCID: PMC389707, DOI: 10.1073/pnas.69.10.3063.Peer-Reviewed Original ResearchInvestigation 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
Temperature dependence of the aminoacylation of tRNA by bacillus stearothermophilus aminoacyl‐tRNA synthetases
Johnson L, Söll D. Temperature dependence of the aminoacylation of tRNA by bacillus stearothermophilus aminoacyl‐tRNA synthetases. Biopolymers 1971, 10: 2209-2221. PMID: 4940767, DOI: 10.1002/bip.360101114.Peer-Reviewed Original ResearchMeSH KeywordsAcylationAmino Acyl-tRNA SynthetasesBacillusChromatography, DEAE-CelluloseEscherichia coliProtein DenaturationRNA, TransferSpectrophotometryTemperatureConceptsSpecific transfer RNAsTRNA-IleTransfer RNAThermal denaturation profilesB. stearothermophilusAminoacyl-tRNA synthetasesDenaturation profilesAminoacylation of tRNAAmino acid acceptor activityTRNA-ValAcceptor activityTRNATertiary structureMycoplasma spBacillus stearothermophilusEscherichia coliAminoacylation reactionStearothermophilusAminoacylationRNASpeciesIleSynthetasesNucleaseSynthetase preparationsA 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, GeneticTobaccoValinePurification 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, GeneticYeastsThe 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
Isolation 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 ResearchPurification 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 FactorsUltracentrifugation
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 terminationBinding