1993
Identification of a 100‐kDa protein associated with nuclear ribonuclease P activity in Schizosaccharomyces pombe
ZIMMERLY S, DRAINAS D, SYLVERS L, Dieter S. Identification of a 100‐kDa protein associated with nuclear ribonuclease P activity in Schizosaccharomyces pombe. The FEBS Journal 1993, 217: 501-507. PMID: 8223594, DOI: 10.1111/j.1432-1033.1993.tb18270.x.Peer-Reviewed Original ResearchConceptsFission yeast Schizosaccharomyces pombeYeast Schizosaccharomyces pombeGlycerol gradient fractionationCross-linking experimentsPrecursor tRNAsSchizosaccharomyces pombeRibonuclease PProtein interactsRNA componentProtein componentsP activityRibonuclease P activityApparent homogeneityDEAE-cellulose chromatographyPhosphocellulose chromatographySpecific fashionProtein
1991
The Escherichia coli hemL gene encodes glutamate 1-semialdehyde aminotransferase
Ilag L, Jahn D, Eggertsson G, Söll D. The Escherichia coli hemL gene encodes glutamate 1-semialdehyde aminotransferase. Journal Of Bacteriology 1991, 173: 3408-3413. PMID: 2045363, PMCID: PMC207952, DOI: 10.1128/jb.173.11.3408-3413.1991.Peer-Reviewed Original ResearchMeSH KeywordsAminolevulinic AcidCentrifugation, Density GradientChromatography, High Pressure LiquidCloning, MolecularDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelEscherichia coliIntramolecular TransferasesIsomerasesMolecular WeightPyridoxal PhosphatePyridoxamineTransformation, GeneticConceptsGlu-tRNA reductaseTRNA-dependent transformationApparent native molecular massMolecular massGlutamyl-tRNA synthetaseNative molecular massAminoglycoside antibiotic kanamycinHemL geneWild-type DNAAuxotrophic phenotypeC5 pathwaySodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisMap positionGSA aminotransferasePhysical mappingSulfate-polyacrylamide gel electrophoresisRate zonal sedimentationGene productsThird enzymeGlycerol gradientsApparent homogeneityAntibiotic kanamycinEscherichia coliPure proteinTwo 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 functional characterization of the Glu-tRNA(Gln) amidotransferase from Chlamydomonas reinhardtii.
Jahn D, Kim Y, Ishino Y, Chen M, Söll D. Purification and functional characterization of the Glu-tRNA(Gln) amidotransferase from Chlamydomonas reinhardtii. Journal Of Biological Chemistry 1990, 265: 8059-8064. PMID: 1970821, DOI: 10.1016/s0021-9258(19)39038-6.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmmoniaAsparagineAzo CompoundsBinding SitesChlamydomonasElectrophoresis, Polyacrylamide GelEnzyme ActivationGlutamatesGlutamic AcidGlutamineMagnesiumMolecular WeightNitrogenous Group TransferasesNorleucinePhosphorylationProtein DenaturationRNA, Transfer, Amino AcylSpectrophotometrySubstrate SpecificityTransferasesConceptsChlamydomonas reinhardtiiGlutamyl-tRNA synthetaseGlycerol gradient sedimentationSodium dodecyl sulfate-polyacrylamide gelsDodecyl sulfate-polyacrylamide gelsAmide donorSulfate-polyacrylamide gelsGlutamine-dependent reactionGlutamine amidotransferasesPresence of ATPGreen algaeSpecific amidotransferaseFunctional characterizationGlutaminyl-tRNAAmidotransferaseLow glutaminase activityApparent MrGradient sedimentationAlpha 2 structureReinhardtiiEnzymeATPGlutaminase activityStable complexesAmmonia-dependent reactionPurification 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
A wheat HMW glutenin subunit gene reveals a highly repeated structure
Sugiyama T, Rafalski A, Peterson D, Söll D. A wheat HMW glutenin subunit gene reveals a highly repeated structure. Nucleic Acids Research 1985, 13: 8729-8737. PMID: 3001648, PMCID: PMC318947, DOI: 10.1093/nar/13.24.8729.Peer-Reviewed Original ResearchConceptsTypical eukaryotic promoterWheat genomic libraryHMW glutenin subunit genesRNA initiation siteGlutenin subunit genesPartial cDNA cloneAmino acid sequenceMature proteinGenomic libraryGlutenin genesEukaryotic promotersCDNA clonesGene sequencesProline contentSubunit geneAcid sequenceGrain endospermInitiation siteQuality of wheatGenesSynthetic oligonucleotidesHigh glutamineMolecular weightProteinClonesFunctional 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
1982
Organization and nucleotide sequence of nuclear 5S rRNA genes in yellow lupin ( Lupinus lutens )
Rafalski J, Wiewiorowski M, SÖll D. Organization and nucleotide sequence of nuclear 5S rRNA genes in yellow lupin ( Lupinus lutens ). Nucleic Acids Research 1982, 10: 7635-7642. PMID: 7155897, PMCID: PMC327035, DOI: 10.1093/nar/10.23.7635.Peer-Reviewed Original Research
1979
Aminoacyl-tRNA Synthetases: General Features and Recognition of Transfer RNAs
Schimmel P, Söll D. Aminoacyl-tRNA Synthetases: General Features and Recognition of Transfer RNAs. Annual Review Of Biochemistry 1979, 48: 601-648. PMID: 382994, DOI: 10.1146/annurev.bi.48.070179.003125.Peer-Reviewed Original Research
1977
A rapid method for preparation of calf spleen exonuclease *
Silverman S, Sōll D. A rapid method for preparation of calf spleen exonuclease *. Nucleic Acids Research 1977, 4: 3511-3517. PMID: 200894, PMCID: PMC342668, DOI: 10.1093/nar/4.10.3511.Peer-Reviewed Original Research
1972
Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli I. PURIFICATION AND PROPERTIES
Lapointe J, Söll D. Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli I. PURIFICATION AND PROPERTIES. Journal Of Biological Chemistry 1972, 247: 4966-4974. PMID: 4341531, DOI: 10.1016/s0021-9258(19)44925-9.Peer-Reviewed Original ResearchAdenosine TriphosphateAlkylationAmino AcidsAmino Acyl-tRNA SynthetasesAnimalsCatalysisCentrifugation, ZonalChromatographyDiphosphatesDrug StabilityElectrophoresisElectrophoresis, DiscEscherichia coliGlutamatesHot TemperatureHydroxyapatitesIsoelectric FocusingMacromolecular SubstancesMolecular WeightOxidation-ReductionPhosphorus IsotopesRabbitsUltracentrifugationN6 - (Δ2 - Isopentenyl) Adenosine: Biosynthesis in vitro in transfer RNA by an enzyme purified from Eschericha coli
Bartz J, Söll D. N6 - (Δ2 - Isopentenyl) Adenosine: Biosynthesis in vitro in transfer RNA by an enzyme purified from Eschericha coli. Biochimie 1972, 54: 31-39. PMID: 4346747, DOI: 10.1016/s0300-9084(72)80035-x.Peer-Reviewed Original Research
1970
N6-(Δ2-isopentenyl)adenosine: Biosynthesis in vitro in transfer RNA by an enzyme purified from escherichia coli
Bartz J, Kline L, Söll D. N6-(Δ2-isopentenyl)adenosine: Biosynthesis in vitro in transfer RNA by an enzyme purified from escherichia coli. Biochemical And Biophysical Research Communications 1970, 40: 1481-1487. PMID: 4326583, DOI: 10.1016/0006-291x(70)90035-5.Peer-Reviewed Original ResearchMeSH KeywordsAdenineAdenine NucleotidesAlkenesAnimalsCentrifugation, Density GradientChromatography, PaperColiphagesEscherichia coliHydrogen-Ion ConcentrationHydrolysisLiverMolecular WeightMycoplasmaNucleosidesOrganophosphorus CompoundsPhosphoric AcidsPolynucleotidesPotassium PermanganateRatsRNA, BacterialRNA, TransferRNA, ViralTransferasesPurification 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