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
1994
Identity switches between tRNAs aminoacylated by class I glutaminyl- and class II aspartyl-tRNA synthetases.
Frugier M, Söll D, Giegé R, Florentz C. Identity switches between tRNAs aminoacylated by class I glutaminyl- and class II aspartyl-tRNA synthetases. Biochemistry 1994, 33: 9912-21. PMID: 8060999, DOI: 10.1021/bi00199a013.Peer-Reviewed Original ResearchConceptsAminoacyl-tRNA synthetasesIdentity nucleotidesHigh-resolution X-ray structuresAminoacyl-tRNA synthetase complexGlutaminyl-tRNA synthetaseAspartyl-tRNA synthetasesAspartyl-tRNA synthetaseGlutamine identityCognate tRNATRNA structureTRNA moleculesTRNAAminoacylation specificitySynthetase complexSpecific aminoacylationConformational changesSynthetasesEscherichia coliYeastSynthetaseNucleotidesE. coliX-ray structureComplex formationColi
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
1984
Transcription Factor Binding Is Limited by the 5′-Flanking Regions of a Drosophila tRNAHis Gene and a tRNAHis Pseudogene
Cooley L, Schaack J, Burke D, Thomas B, Söll D. Transcription Factor Binding Is Limited by the 5′-Flanking Regions of a Drosophila tRNAHis Gene and a tRNAHis Pseudogene. Molecular And Cellular Biology 1984, 4: 2714-2722. DOI: 10.1128/mcb.4.12.2714-2722.1984.Peer-Reviewed Original ResearchDrosophila Kc cell extractHeLa cell extractsTRNAHis geneCell extractsReal genesStable complex formationControl regionDeletion analysisStable transcription complex formationRecombinant clonesDrosophila tRNAArg geneTRNA gene clusterTranscription complex formationBona fide genesInternal control regionTranscription factor bindingSame DNA strandComplex formationTranscription control regionsConsecutive base pairsTRNAArg geneFide genesGene clusterTranscription factorsFactor bindingTranscription factor binding is limited by the 5'-flanking regions of a Drosophila tRNAHis gene and a tRNAHis pseudogene.
Cooley L, Schaack J, Burke DJ, Thomas B, Söll D. Transcription factor binding is limited by the 5'-flanking regions of a Drosophila tRNAHis gene and a tRNAHis pseudogene. Molecular And Cellular Biology 1984, 4: 2714-2722. PMID: 6570190, PMCID: PMC369281, DOI: 10.1128/mcb.4.12.2714.Peer-Reviewed Original ResearchConceptsDrosophila Kc cell extractHeLa cell extractsCell extractsReal genesStable complex formationControl regionDeletion analysisStable transcription complex formationRecombinant clonesDrosophila tRNAArg geneTRNA gene clusterTranscription complex formationBona fide genesInternal control regionTranscription factor bindingSame DNA strandComplex formationTranscription control regionsConsecutive base pairsTRNAHis geneTRNAArg geneFide genesGene clusterTranscription factorsFactor bindingThe extent of a eukaryotic tRNA gene. 5‘- and 3‘-flanking sequence dependence for transcription and stable complex formation.
Schaack J, Sharp S, Dingermann T, Burke DJ, Cooley L, Söll D. The extent of a eukaryotic tRNA gene. 5‘- and 3‘-flanking sequence dependence for transcription and stable complex formation. Journal Of Biological Chemistry 1984, 259: 1461-1467. PMID: 6693417, DOI: 10.1016/s0021-9258(17)43429-6.Peer-Reviewed Original ResearchConceptsStable complex formationBase pairsDrosophila Kc cell extractSequence requirementsCell extractsEukaryotic tRNA genesStable transcription complexesHeLa cell extractsTRNA genesComplex formationTranscription complexArg genesEfficient transcriptionTranscription assaysTranscription propertiesCell-free extractsTranscriptionHomologous systemGenesSequenceSequence dependenceCellular sourceExtractAssaysPairs
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 ResearchConceptsS 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 chromatographyTranscription 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
1972
Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli II. INTERACTION WITH INTACT GLUTAMYL TRANSFER RIBONUCLEIC ACID
Lapointe J, Söll D. Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli II. INTERACTION WITH INTACT GLUTAMYL TRANSFER RIBONUCLEIC ACID. Journal Of Biological Chemistry 1972, 247: 4975-4981. PMID: 4341532, DOI: 10.1016/s0021-9258(19)44926-0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acyl-tRNA SynthetasesCarbon IsotopesCatalysisCentrifugation, Density GradientDiphosphatesDrug StabilityEscherichia coliGlutamatesHot TemperatureHydrogen-Ion ConcentrationKineticsLeucineMagnesiumPhosphorus IsotopesProtein BindingRNA, TransferSpectrometry, FluorescenceValineConceptsGlutamyl-transfer ribonucleic acid synthetaseEscherichia coli IITransfer ribonucleic acidTRNA-GluTRNA-ValTRNA-LeuCognate tRNABiological specificityRibonucleic acidPure enzymeEnzymeSimilar Km valuesComplex formationGradient centrifugationSynthetaseKm valuesFluorescence-quenching studiesTRNAIsoacceptorsComplexesFluorescence quenching studiesHeat inactivationInactivationLeuGlu
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