2004
The unusual methanogenic seryl‐tRNA synthetase recognizes tRNASer species from all three kingdoms of life
Bilokapic S, Korencic D, Söll D, Weygand‐Durasevic I. The unusual methanogenic seryl‐tRNA synthetase recognizes tRNASer species from all three kingdoms of life. The FEBS Journal 2004, 271: 694-702. PMID: 14764085, DOI: 10.1111/j.1432-1033.2003.03971.x.Peer-Reviewed Original ResearchMeSH KeywordsAnticodonBase SequenceChromatography, GelDimerizationElectrophoretic Mobility Shift AssayEscherichia coliIsoelectric FocusingMethanococcusMolecular Sequence DataNucleic Acid ConformationProtein BindingRNA, Transfer, Amino AcylRNA, Transfer, SerSerineSerine-tRNA LigaseSubstrate SpecificityTranscription, GeneticYeastsConceptsSeryl-tRNA synthetaseGel mobility shift assaysKingdoms of lifeMobility shift assaysMethanococcus jannaschiiM. maripaludisTRNA recognitionShift assaysTRNARenaturation conditionsGel filtration chromatographyConformation of tRNAComplex formationSpeciesFiltration chromatographySynthetaseDimerizationSerRSsJannaschiiTRNASerIsoacceptorsHomologuesComplementary oligonucleotidesAminoacylationRenaturation
1992
Glutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression.
Verkamp E, Jahn M, Jahn D, Kumar A, Söll D. Glutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression. Journal Of Biological Chemistry 1992, 267: 8275-8280. PMID: 1569081, DOI: 10.1016/s0021-9258(18)42438-6.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde OxidoreductasesAmino Acid SequenceBase SequenceChromatography, GelCyanobacteriaEscherichia coliGene ExpressionGenes, BacterialGenes, FungalGenetic Complementation TestMolecular Sequence DataOpen Reading FramesPlasmidsRestriction MappingSaccharomyces cerevisiaeSequence Homology, Nucleic AcidConceptsGlutamyl-tRNA reductaseHemA geneAmino acid sequenceHemA proteinGluTR activitySynechocystis 6803Acid sequenceE. coliGlutamate-1-semialdehyde aminotransferaseHemA gene productEscherichia coliCyanobacterium Synechocystis spOpen reading frameEnterobacterium Escherichia coliDNA sequence analysisFunctional complementationGene structureGlu-tRNAGel filtration experimentsPCC 6803Synechocystis spGlutamyl-tRNAAcid polypeptideReading frameALA formation
1991
Two glutamyl-tRNA reductase activities in Escherichia coli
Jahn D, Michelsen U, Söll D. Two glutamyl-tRNA reductase activities in Escherichia coli. Journal Of Biological Chemistry 1991, 266: 2542-2548. PMID: 1990004, DOI: 10.1016/s0021-9258(18)52279-1.Peer-Reviewed Original ResearchConceptsReductase activityGlu-tRNA reductaseMolecular massEscherichia coliApparent molecular massDifferent chromatographic separationsSequence-specific recognitionGlycerol gradient centrifugationThree-step conversionTetrapyrrole biosynthesisChlamydomonas reinhardtiiE. coli K12ALA formationChromatographic separationKey enzymeMonomeric structureActive enzymeBacillus subtilisColi K12Nondenaturing conditionsHomogeneous proteinMolecular weightDelta-aminolevulinic acidEnzyme activityAddition of GTPPurification 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 groups
1985
Functional analysis of fractionated Drosophila Kc cell tRNA gene transcription components.
Burke D, Söll D. Functional analysis of fractionated Drosophila Kc cell tRNA gene transcription components. Journal Of Biological Chemistry 1985, 260: 816-823. PMID: 3844013, DOI: 10.1016/s0021-9258(20)71171-3.Peer-Reviewed Original ResearchConceptsTranscription componentsTRNA genesDrosophila Kc cell extractFunctional analysisActive transcription complexesHuman HeLa cellsFactor BDrosophila systemTranscription initiationStable complex formationTranscription complexC associatesLarge complexesReconstitution experimentsCell extractsHeLa cellsCell factorFactor C.Factor CGenesStable complexesComplex formationPartial purificationComplexesDNA
1972
Investigation 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
Purification 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 bufferSequence
1970
The 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