2009
The Human SepSecS-tRNASec Complex Reveals the Mechanism of Selenocysteine Formation
Palioura S, Sherrer RL, Steitz TA, Söll D, Simonović M. The Human SepSecS-tRNASec Complex Reveals the Mechanism of Selenocysteine Formation. Science 2009, 325: 321-325. PMID: 19608919, PMCID: PMC2857584, DOI: 10.1126/science.1173755.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesBase SequenceBiocatalysisCatalytic DomainCrystallography, X-RayHumansHydrogen BondingModels, MolecularMolecular Sequence DataNucleic Acid ConformationPhosphatesPhosphoserineProtein ConformationProtein MultimerizationProtein Structure, SecondaryRNA, Transfer, Amino Acid-SpecificRNA, Transfer, Amino AcylSelenocysteineConceptsTransfer RNASelenocysteine formationSelenocysteinyl-tRNA synthaseCognate transfer RNAEnzyme active siteTRNA bindingActive siteConformational changesEnzyme assaysAmino acidsFree phosphoserinePhosphoserineSepSecSFinal stepSelenocysteineBiosynthesisComplexesRNAMechanismBindsCrystal structureSynthaseBindingFormationAssays
1992
Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation
Sherman J, Rogers M, Söll D. Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation. Nucleic Acids Research 1992, 20: 2847-2852. PMID: 1377381, PMCID: PMC336931, DOI: 10.1093/nar/20.11.2847.Peer-Reviewed Original ResearchConceptsAccuracy of aminoacylationAminoacyl-tRNA synthetasesTyrosyl-tRNA synthetaseE. coli tyrosyl-tRNA synthetaseEscherichia coli tyrosyl-tRNA synthetaseGlutaminyl-tRNA synthetaseLevel of aminoacylationProtein biosynthesisTRNASynthetasesAminoacylationCompetition assaysDiscriminator baseDifferent synthetasesConcurrent overexpressionCorrect aminoacylationSynthetaseFirst baseRelative affinityVivoMisacylationAssaysAnticodonBiosynthesisCompetitionCompetition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation
Sherman J, Rogers M, Söll D. Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation. Nucleic Acids Research 1992, 20: 1547-1552. PMID: 16617497, PMCID: PMC312236, DOI: 10.1093/nar/20.7.1547.Peer-Reviewed Original ResearchAccuracy of aminoacylationAminoacyl-tRNA synthetasesTyrosyl-tRNA synthetaseE. coli tyrosyl-tRNA synthetaseEscherichia coli tyrosyl-tRNA synthetaseGlutaminyl-tRNA synthetaseLevel of aminoacylationProtein biosynthesisTRNASynthetasesAminoacylationCompetition assaysDiscriminator baseDifferent synthetasesConcurrent overexpressionCorrect aminoacylationSynthetaseFirst baseRelative affinityVivoMisacylationAssaysAnticodonBiosynthesisCompetition
1990
Inaccuracy and the Recognition of †RNA
Rogers M, Soll D. Inaccuracy and the Recognition of †RNA. Progress In Nucleic Acid Research And Molecular Biology 1990, 39: 185-208. PMID: 2247608, DOI: 10.1016/s0079-6603(08)60627-3.Peer-Reviewed Original ResearchConceptsATP-dependent stepNoncognate aminoacyl-tRNAsGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetasesRecognition of tRNAAmber mutationGlnRAminoacyl-tRNAEditing mechanismTRNAMutantsMischargingCentral roleEnzymeSynthetasesMisaminoacylationSupF.SupFSynthetaseMutationsGlutamineMechanismSuppressionAssays
1984
The 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