2011
Rational design of an evolutionary precursor of glutaminyl-tRNA synthetase
O’Donoghue P, Sheppard K, Nureki O, Söll D. Rational design of an evolutionary precursor of glutaminyl-tRNA synthetase. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 20485-20490. PMID: 22158897, PMCID: PMC3251134, DOI: 10.1073/pnas.1117294108.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acyl-tRNA SynthetasesBase SequenceCodonEscherichia coliEvolution, MolecularGenetic EngineeringKineticsMethanobacteriaceaeModels, MolecularMolecular ConformationMolecular Sequence DataNucleic Acid ConformationPhylogenyProtein Structure, SecondarySequence Homology, Amino AcidConceptsGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetasesGenetic code engineeringAmino acidsDomains of lifeMost aminoacyl-tRNA synthetasesGlutamyl-tRNA synthetaseCanonical amino acidsBacterial GlnRSTRNA specificityTRNA pairsParticular codonsEvolutionary precursorBiochemical characterizationStem loopGlnRAdditional codonsCAA codonCodonProtein synthesisCAG codonEscherichia coliSpecific enzymesCatalytic preferenceSynthetase
2008
Characterization and evolutionary history of an archaeal kinase involved in selenocysteinyl-tRNA formation
Sherrer RL, O’Donoghue P, Söll D. Characterization and evolutionary history of an archaeal kinase involved in selenocysteinyl-tRNA formation. Nucleic Acids Research 2008, 36: 1247-1259. PMID: 18174226, PMCID: PMC2275090, DOI: 10.1093/nar/gkm1134.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAdenosine TriphosphateAmino Acid SequenceArchaeal ProteinsBinding SitesEvolution, MolecularKineticsMethanococcalesModels, MolecularMutationPhosphotransferasesPhylogenyProtein Structure, TertiaryRNA, Transfer, Amino AcylSequence AlignmentSingle-Strand Specific DNA and RNA EndonucleasesSubstrate SpecificityConceptsATPase active sitePhosphate-binding loopInduced fit mechanismRxxxR motifEvolutionary historyWalker BKinase familyPhylogenetic analysisSep-tRNARelated kinasesPSTKBiochemical characterizationSynthase convertsFit mechanismKinaseATPase activityPlasmodium speciesMotifActive siteSerHigh affinityDecreased activityArchaeaSepSecSSer18
2002
A one‐step method for in vitro production of tRNA transcripts
Korencić D, Söll D, Ambrogelly A. A one‐step method for in vitro production of tRNA transcripts. Nucleic Acids Research 2002, 30: e105-e105. PMID: 12384607, PMCID: PMC137149, DOI: 10.1093/nar/gnf104.Peer-Reviewed Original ResearchConceptsTRNA transcriptsT7 RNA polymeraseLarge-scale plasmid preparationTRNA genesMicrobial genomesTRNA functionsDNA promoterRNA polymeraseRNA moleculesT7 promoterBiochemical characterizationTranscription templateDNA templateNew enzymeTranscriptsLarge oligonucleotidesTranscriptionGood substratePromoterShort oligonucleotidesEnzymatic digestionRapid productionPlasmid preparationsGenomeOligonucleotide
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