1994
Thiobacillus ferrooxidans tyrosyl-tRNA synthetase functions in vivo in Escherichia coli
Salazar O, Sagredo B, Jedlicki E, Söll D, Weygand-Durasevic I, Orellana O. Thiobacillus ferrooxidans tyrosyl-tRNA synthetase functions in vivo in Escherichia coli. Journal Of Bacteriology 1994, 176: 4409-4415. PMID: 7517395, PMCID: PMC205654, DOI: 10.1128/jb.176.14.4409-4415.1994.Peer-Reviewed Original ResearchMeSH KeywordsAcidithiobacillus thiooxidansAmino Acid SequenceBase SequenceGene Expression Regulation, BacterialGenes, BacterialGenetic Complementation TestMolecular Sequence DataMutationNucleic Acid HybridizationOperonPromoter Regions, GeneticRNA, BacterialRNA, RibosomalRNA, Transfer, TyrSequence Analysis, DNATyrosine-tRNA LigaseConceptsOverall identityTyrosyl-tRNA synthetase geneRho-independent transcription terminatorEscherichia coli TyrRSClass I aminoacyl-tRNA synthetasesRibosomal RNA operonSingle-copy geneAminoacyl-tRNA synthetasesTyrosyl-tRNA synthetasesSouthern blot analysisRNA operonBioleaching of mineralsThermosensitive mutationTranscription unitTranscription terminatorSynthetase genePutative promoterProtein sequencesSynthetase functionE. coli strainsGenesSignature sequencesEscherichia coliAmino acidsDNA probes
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
Each element of the Drosophila tRNA Arg gene split promoter directs transcription in Xenopus oocytes
Sharp S, Dingermann T, Schaack J, Sharp J, Burke D, DeRobertis E, Söll D. Each element of the Drosophila tRNA Arg gene split promoter directs transcription in Xenopus oocytes. Nucleic Acids Research 1983, 11: 8677-8690. PMID: 6561520, PMCID: PMC326616, DOI: 10.1093/nar/11.24.8677.Peer-Reviewed Original ResearchConceptsD-control regionDrosophila tRNAArg geneTRNAArg geneEukaryotic tRNA gene transcriptionXenopus oocytesRNA polymerase III transcription factorT-control regionEukaryotic tRNA genesTRNA gene transcriptionIntragenic control regionTranscription initiation siteSpecific DNA sequencesTRNA genesTranscription initiationArg genesControl regionTranscription factorsGene transcriptionDNA sequencesMutant formsOocyte nucleusSequence 5Initiation siteGenesTranscription
1979
Regulation of biosynthesis of aminoacyl-transfer RNA synthetases and of transfer-RNA in Escherichia coli.
Morgan S, Larossa R, Cheung A, Low B, Söll D. Regulation of biosynthesis of aminoacyl-transfer RNA synthetases and of transfer-RNA in Escherichia coli. Biological Research 1979, 12: 415-26. PMID: 45219.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseLeucyl-tRNA synthetaseGlnR mutantRegulation of biosynthesisClasses of mutantsTemperature-resistant revertantsOperator-promoter regionAminoacyl-transfer RNA synthetasesStructural geneLeu genesRegulatory mutantsThermolabile leucyl-tRNA synthetaseMutantsResistant revertantsFormation of glutamineGlutamine synthetaseE. coli strainsEscherichia coliRNA synthetasesGenesSynthetaseElevated levelsRevertantsColi strainsGlnT
1977
Regulation of biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coli III. Biochemical characterization of regulatory mutants affecting leucyl-tRNA synthetase levels
LaRossa R, Mao J, Low K, Söll D. Regulation of biosynthesis of aminoacyl-tRNA synthetases and of tRNA in Escherichia coli III. Biochemical characterization of regulatory mutants affecting leucyl-tRNA synthetase levels. Journal Of Molecular Biology 1977, 117: 1049-1059. PMID: 342704, DOI: 10.1016/s0022-2836(77)80012-0.Peer-Reviewed Original ResearchConceptsAminoacyl-tRNA synthetasesLeucyl-tRNA synthetaseProtein synthesisRegulation of biosynthesisEscherichia coli IIIIsoacceptor familiesIlv operonRegulatory mutantsSteady-state levelsAmount of tRNALeu operonBiochemical characterizationCellular concentrationSynthetasesEscherichia coliOperonControl elementsTRNASynthetaseSynthetase levelsMutationsDerepressionPpGppMutantsPppGpp