2012
Yeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignment
Ling J, Peterson KM, Simonović I, Cho C, Söll D, Simonović M. Yeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignment. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 3281-3286. PMID: 22343532, PMCID: PMC3295322, DOI: 10.1073/pnas.1200109109.Peer-Reviewed Original ResearchMeSH KeywordsAeropyrumAmino Acid SequenceAnticodonCatalytic DomainCodonCrystallography, X-RayEscherichia coliEvolution, MolecularLeucineMitochondriaModels, MolecularMolecular Sequence DataProtein ConformationProtein Structure, TertiaryRNA EditingRNA, Transfer, Amino AcylSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSpecies SpecificityStaphylococcus aureusSubstrate SpecificityThreonineThreonine-tRNA LigaseConceptsThreonyl-tRNA synthetaseAnticodon loopAnticodon sequenceEscherichia coli ThrRSSet of tRNAsDistinct recognition mechanismsAnticodon-binding domainAminoacyl-tRNA synthetasesCUN codonsDetailed structural comparisonCodon reassignmentYeast mitochondriaGenetic codeTRNA isoacceptorsSaccharomyces cerevisiaeIsoacceptor tRNAsEditing domainTRNAMST1Anticodon tripletStructural comparisonNatural tRNAAmino acidsDistinct mechanismsRecognition mechanism
2010
Structure of an archaeal non-discriminating glutamyl-tRNA synthetase: a missing link in the evolution of Gln-tRNAGln formation
Nureki O, O’Donoghue P, Watanabe N, Ohmori A, Oshikane H, Araiso Y, Sheppard K, Söll D, Ishitani R. Structure of an archaeal non-discriminating glutamyl-tRNA synthetase: a missing link in the evolution of Gln-tRNAGln formation. Nucleic Acids Research 2010, 38: 7286-7297. PMID: 20601684, PMCID: PMC2978374, DOI: 10.1093/nar/gkq605.Peer-Reviewed Original ResearchConceptsNon-discriminating glutamyl-tRNA synthetaseGlutamyl-tRNA synthetaseND-GluRSEscherichia coli GlnRSFormation of GlnCognate tRNA moleculesGlutaminyl-tRNA synthetaseAnticodon-binding domainEvolutionary predecessorPhylogenetic analysisGenetic codeMolecular basisTRNA moleculesRecognition pocketGlnRGenetic encodingAmino acidsSpecific ligationStructural determinantsKey eventsSynthetaseGluPromiscuous recognitionGluRGln
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 structureSynthaseBindingFormationAssaysA Cytidine Deaminase Edits C to U in Transfer RNAs in Archaea
Randau L, Stanley BJ, Kohlway A, Mechta S, Xiong Y, Söll D. A Cytidine Deaminase Edits C to U in Transfer RNAs in Archaea. Science 2009, 324: 657-659. PMID: 19407206, PMCID: PMC2857566, DOI: 10.1126/science.1170123.Peer-Reviewed Original ResearchConceptsTransfer RNAArchaeon Methanopyrus kandleriTertiary coreCytidine deaminase domainsTRNA genesTransfer RNAsTHUMP domainProper foldingU editingC deaminationMethanopyrus kandleriTRNA tertiary structureDeaminase domainTertiary structureTRNA tertiary corePosition 8Cytidine deaminaseUnique familyArchaeaRNAsGenesRNAFoldingDomainCrystal structure