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
1993
Discrimination among tRNAs intermediate in glutamate and glutamine acceptor identity.
Rogers K, Söll D. Discrimination among tRNAs intermediate in glutamate and glutamine acceptor identity. Biochemistry 1993, 32: 14210-9. PMID: 7505112, DOI: 10.1021/bi00214a021.Peer-Reviewed Original ResearchAmino Acyl-tRNA SynthetasesAnticodonBase SequenceBiological EvolutionEscherichia coliGlutamate-tRNA LigaseHydrogen BondingKineticsMolecular Sequence DataNucleic Acid ConformationRNA, BacterialRNA, Transfer, GlnRNA, Transfer, GluStructure-Activity RelationshipSubstrate SpecificityTransfer RNA Aminoacylation
1992
Recognition of bases in Escherichia coli tRNA(Gln) by glutaminyl‐tRNA synthetase: a complete identity set.
Hayase Y, Jahn M, Rogers M, Sylvers L, Koizumi M, Inoue H, Ohtsuka E, Söll D. Recognition of bases in Escherichia coli tRNA(Gln) by glutaminyl‐tRNA synthetase: a complete identity set. The EMBO Journal 1992, 11: 4159-4165. PMID: 1396597, PMCID: PMC556926, DOI: 10.1002/j.1460-2075.1992.tb05509.x.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseRecognition of basesSet of tRNAsEscherichia coliCognate aminoacyl-tRNA synthetasesAminoacyl-tRNA synthetasesCorrect aminoacylationRecombinant RNA technologySet of nucleotidesNumber of mutantsGlutamine identityTRNA genesTRNA discriminationTransfer RNAExcellent systemGlnRFunctional importanceSingle deletionSpecific contactsRNA technologyBase changesSpecificity constantAminoacylationSpecific guanosineMutants
1989
Structural Basis for Misaminoacylation by Mutant E. coli Glutaminyl-tRNA Synthetase Enzymes
Perona J, Swanson R, Rould M, Steitz T, Söll D. Structural Basis for Misaminoacylation by Mutant E. coli Glutaminyl-tRNA Synthetase Enzymes. Science 1989, 246: 1152-1154. PMID: 2686030, DOI: 10.1126/science.2686030.Peer-Reviewed Original Research
1984
The sup8 tRNALeu gene of Schizosaccharomyces pombe has an unusual intervening sequence and reduced pairing in the anticodon stem
Sumner-Smith M, Hottinger H, Willis I, Koch T, Arentzen R, Söll D. The sup8 tRNALeu gene of Schizosaccharomyces pombe has an unusual intervening sequence and reduced pairing in the anticodon stem. Molecular Genetics And Genomics 1984, 197: 447-452. PMID: 6597338, DOI: 10.1007/bf00329941.Peer-Reviewed Original ResearchConceptsTRNA genesS. pombe DNAWild-type alleleAnticodon UCASplicing endonucleaseSuppressor allelesSchizosaccharomyces pombeTRNALeu geneUUA codonTrailer sequencesIntervening sequenceCell-free extractsAnticodon stemRelated sequencesSplice siteBase pairsSecondary structureGenesIsoacceptorsAllelesSequenceStructural requirementsPombeAnticodonSup8