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 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
1989
A selection for mutants of the RNA polymerase III transcription apparatus: PCF1 stimulates transcription of tRNA and 5S RNA genes.
Willis I, Schmidt P, Söll D. A selection for mutants of the RNA polymerase III transcription apparatus: PCF1 stimulates transcription of tRNA and 5S RNA genes. The EMBO Journal 1989, 8: 4281-4288. PMID: 2686985, PMCID: PMC401634, DOI: 10.1002/j.1460-2075.1989.tb08614.x.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceCloning, MolecularDNA-Directed RNA PolymerasesGene ExpressionGenes, DominantGenes, FungalKineticsMolecular Sequence DataMutationOligonucleotide ProbesPlasmidsPromoter Regions, GeneticRNA Polymerase IIIRNA, RibosomalRNA, Ribosomal, 5SRNA, TransferSaccharomyces cerevisiaeSaccharomycetalesSchizosaccharomycesSelection, GeneticSuppression, GeneticTemplates, GeneticTranscription, GeneticConceptsTRNA genesMutant strainTranscription of mutantsTranscription of tRNARNA polymerase IIISuppressor tRNA geneDominant mutant geneWild-type strainStable complexesTranscription apparatusRNA genesStable complex formationUpstream geneTRNA suppressorsPositive regulatorSteady-state levelsComplex assemblyGenetic approachesPolymerase IIIGene transcriptionInternal promoterMutant geneTime-course experimentsTranscriptionGenes
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
1983
Transcription of eukaryotic tRNA genes in vitro. II. Formation of stable complexes.
Schaack J, Sharp S, Dingermann T, Söll D. Transcription of eukaryotic tRNA genes in vitro. II. Formation of stable complexes. Journal Of Biological Chemistry 1983, 258: 2447-2453. PMID: 6549758, DOI: 10.1016/s0021-9258(18)32946-6.Peer-Reviewed Original ResearchConceptsStable transcription complex formationTRNA genesTranscription complex formationStable transcription complexesTranscription complexDrosophila Kc cell extractGene regionD-stemDrosophila tRNAArg geneEukaryotic tRNA genesDrosophila tRNA genesTranscription termination sequenceTRNAArg geneStable complexesComplex formationTranscription experimentsDNA regionsTranscription factorsFactor bindingCell-free extractsTermination sequenceSequence 5T-stemCell extractsDeletion mutations
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