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
1983
Partial purification of Drosophila Kc cell RNA polymerase III transcription components. Evidence for shared 5 S RNA and tRNA gene factors.
Burke D, Schaack J, Sharp S, Söll D. Partial purification of Drosophila Kc cell RNA polymerase III transcription components. Evidence for shared 5 S RNA and tRNA gene factors. Journal Of Biological Chemistry 1983, 258: 15224-15231. PMID: 6197413, DOI: 10.1016/s0021-9258(17)43797-5.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsChromatography, Ion ExchangeDNA-Directed RNA PolymerasesDrosophilaElectrophoresis, Polyacrylamide GelRNARNA Polymerase IIIRNA, TransferRNA, Transfer, Amino AcylTranscription, GeneticConceptsS RNA geneTranscription componentsRNA polymerase IIIRNA genesPolymerase IIIStable transcription complex formationReconstitution of transcriptionTranscription complex formationDrosophila Kc cellsCM-Sepharose column chromatographyDrosophila tRNAKc cellsTranscription factorsS RNATRNAGene factorsCompetition experimentsTranscriptionGenesComplex formationPartial purificationDEAE-SephadexReconstitutionCofractionationColumn chromatography
1974
Involvement of the anticodon region of Escherichia coli tRNAGln and tRNAGlu in the specific interaction with cognate aminoacyl-tRNA synthetase Alteration of the 2-thiouridine derivatives located in the anticodon of the tRNAs by BrCN or sulfur deprivation
Seno T, Agris P, Söll D. Involvement of the anticodon region of Escherichia coli tRNAGln and tRNAGlu in the specific interaction with cognate aminoacyl-tRNA synthetase Alteration of the 2-thiouridine derivatives located in the anticodon of the tRNAs by BrCN or sulfur deprivation. Biochimica Et Biophysica Acta 1974, 349: 328-338. PMID: 4366808, DOI: 10.1016/0005-2787(74)90120-8.Peer-Reviewed Original ResearchAdenosine TriphosphateAmino Acyl-tRNA SynthetasesCarbon RadioisotopesChromatography, Ion ExchangeCyanogen BromideDiphosphatesEscherichia coliGlutamatesGlutamineKineticsPhosphorus RadioisotopesProtein BiosynthesisRNA, BacterialRNA, TransferSpectrophotometry, UltravioletThiouridineTransfer RNA AminoacylationN‐(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
1973
Biological function of 2-thiouridine in Escherichia coli glutamic acid transfer ribonucleic acid.
Agris P, Soell D, Seno T. Biological function of 2-thiouridine in Escherichia coli glutamic acid transfer ribonucleic acid. Biochemistry 1973, 12: 4331-7. PMID: 4584321, DOI: 10.1021/bi00746a005.Peer-Reviewed Original ResearchAmino Acyl-tRNA SynthetasesCarbon RadioisotopesChromatography, Ion ExchangeChromatography, Thin LayerCyanogen BromideElectrophoresis, DiscElectrophoresis, Polyacrylamide GelEscherichia coliGlutamatesKineticsMutationProtein BiosynthesisRNA, BacterialRNA, TransferSpectrophotometry, UltravioletSulfurSulfur RadioisotopesThiouridineTritium
1971
A 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 bufferSequence
1970
Purification 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
Biosynthesis 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 synthesisFractionation of Escherichia coli transfer RNA on benzoylated DEAE-cellulose
Roy K, Söll D. Fractionation of Escherichia coli transfer RNA on benzoylated DEAE-cellulose. Biochimica Et Biophysica Acta 1968, 161: 572-574. PMID: 4875424, DOI: 10.1016/0005-2787(68)90137-8.Peer-Reviewed Original Research