2008
Pyrrolysyl-tRNA synthetase–tRNAPyl structure reveals the molecular basis of orthogonality
Nozawa K, O’Donoghue P, Gundllapalli S, Araiso Y, Ishitani R, Umehara T, Söll D, Nureki O. Pyrrolysyl-tRNA synthetase–tRNAPyl structure reveals the molecular basis of orthogonality. Nature 2008, 457: 1163-1167. PMID: 19118381, PMCID: PMC2648862, DOI: 10.1038/nature07611.Peer-Reviewed Original ResearchConceptsAmino acidsMolecular basisLast universal common ancestorUniversal common ancestorUAG stop codonProteinogenic amino acidsCommon ancestorSuppressor tRNAStop codonDesulfitobacterium hafnienseStandard amino acidsTRNADistinct interactionsProteinPyrrolysinePylRSSelenocysteineAncestorCodonMachineryAcidVivoPairs
1997
Glutaminyl-tRNA synthetase.
Freist W, Gauss D, Ibba M, Söll D. Glutaminyl-tRNA synthetase. Biological Chemistry 1997, 378: 1103-17. PMID: 9372179.Peer-Reviewed Original ResearchConceptsE. coli GlnRSGlutaminyl-tRNA synthetaseGlutamyl-tRNA synthetaseMammalian enzymeCommon ancestorPositive eubacteriaCognate tRNAMultienzyme complexTRNA moleculesGlnRArtificial mutantsAcceptor stemAnticodon loopMolecular massAmino acidsCatalytic siteEnzymeSynthetaseEubacteriaArchaebacteriaTRNAMutantsOrganellesAncestorComplexes
1993
Selection of a ‘minimal’ glutaminyl‐tRNA synthetase and the evolution of class I synthetases.
Schwob E, Söll D. Selection of a ‘minimal’ glutaminyl‐tRNA synthetase and the evolution of class I synthetases. The EMBO Journal 1993, 12: 5201-5208. PMID: 7505222, PMCID: PMC413784, DOI: 10.1002/j.1460-2075.1993.tb06215.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesBacterial ProteinsBase SequenceBinding SitesBiological EvolutionEscherichia coliModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein Structure, TertiaryRNA, BacterialRNA, Transfer, GlnRNA, Transfer, SerStructure-Activity RelationshipTransfer RNA AminoacylationConceptsGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetasesEscherichia coli glutaminyl-tRNA synthetaseClass I aminoacyl-tRNA synthetasesNew recognition specificitiesNon-catalytic domainSubstrate recognition propertiesNon-cognate tRNAsRecognition of tRNACommon ancestorSequence motifsAmber suppressorGenetic codeTRNA substratesCatalytic coreGlnRTRNARecognition specificityDistinct domainsEnzymatic activityElaborate relationshipSynthetasesSpecific roleClass ISynthetase
1985
Nucleotide sequences of two serine tRNAs with a GGA anticodon: the structure-function relationships in the serine family of E. coli tRNAs
Grosjean H, Nicoghosian K, Haumont E, Söll D, Cedergren R. Nucleotide sequences of two serine tRNAs with a GGA anticodon: the structure-function relationships in the serine family of E. coli tRNAs. Nucleic Acids Research 1985, 13: 5697-5706. PMID: 3898020, PMCID: PMC321899, DOI: 10.1093/nar/13.15.5697.Peer-Reviewed Original ResearchConceptsSerine tRNANucleotide sequenceRecent common ancestorE. coli tRNACodon-anticodon interactionStructure-function relationshipsEubacterial originUCU codonsEvolutionary analysisCommon ancestorD-loopTRNAAnticodon stemSerine familyAnticodonGenesE. coliMinor speciesCodonMajor speciesSpeciesSequenceTRNASerAncestorSerine