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
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