2011
Rational design of an evolutionary precursor of glutaminyl-tRNA synthetase
O’Donoghue P, Sheppard K, Nureki O, Söll D. Rational design of an evolutionary precursor of glutaminyl-tRNA synthetase. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 20485-20490. PMID: 22158897, PMCID: PMC3251134, DOI: 10.1073/pnas.1117294108.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acyl-tRNA SynthetasesBase SequenceCodonEscherichia coliEvolution, MolecularGenetic EngineeringKineticsMethanobacteriaceaeModels, MolecularMolecular ConformationMolecular Sequence DataNucleic Acid ConformationPhylogenyProtein Structure, SecondarySequence Homology, Amino AcidConceptsGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetasesGenetic code engineeringAmino acidsDomains of lifeMost aminoacyl-tRNA synthetasesGlutamyl-tRNA synthetaseCanonical amino acidsBacterial GlnRSTRNA specificityTRNA pairsParticular codonsEvolutionary precursorBiochemical characterizationStem loopGlnRAdditional codonsCAA codonCodonProtein synthesisCAG codonEscherichia coliSpecific enzymesCatalytic preferenceSynthetase
1988
Site-directed mutagenesis to fine-tune enzyme specificity
Uemura H, Rogers M, Swanson R, Watson L, Söll D. Site-directed mutagenesis to fine-tune enzyme specificity. Protein Engineering Design And Selection 1988, 2: 293-296. PMID: 3150543, DOI: 10.1093/protein/2.4.293.Peer-Reviewed Original ResearchConceptsOligonucleotide-directed mutagenesisEscherichia coli glutaminyl-tRNA synthetaseGenetic selectionGlutaminyl-tRNA synthetaseAmino acid replacementsSite-directed mutagenesisAcid replacementsEnzyme specificitySingle residueMutagenesisSide chainsRepulsive charge-charge interactionsSpecific recognitionCharge-charge interactionsNucleic acidsMutantsProteinSupFSynthetaseResiduesGlutamineSelection