2020
Initiation of Protein Synthesis with Non‐Canonical Amino Acids In Vivo
Tharp J, Ad O, Amikura K, Ward F, Garcia E, Cate J, Schepartz A, Söll D. Initiation of Protein Synthesis with Non‐Canonical Amino Acids In Vivo. Angewandte Chemie 2020, 132: 3146-3150. DOI: 10.1002/ange.201914671.Peer-Reviewed Original ResearchNon-canonical amino acidsDistinct non-canonical amino acidsE. coli translational machineryAmino acidsNon-canonical initiationTRNA fMetTranslational machineryInitiator tRNASynthetic biologyE. coli strainsProtein synthesisDiverse sidechainsColi strainsFMetRemarkable versatilityVivoInitial stepSecond positionGenomeTyrRSTRNARedundant copiesMachineryBiologyPolypeptide
2001
Conserved amino acids near the carboxy terminus of bacterial tyrosyl‐tRNA synthetase are involved in tRNA and Tyr‐AMP binding
Salazar J, Zuñiga R, Lefimil C, Söll D, Orellana O. Conserved amino acids near the carboxy terminus of bacterial tyrosyl‐tRNA synthetase are involved in tRNA and Tyr‐AMP binding. FEBS Letters 2001, 491: 257-260. PMID: 11240138, DOI: 10.1016/s0014-5793(01)02214-1.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine MonophosphateBacterial ProteinsCloning, MolecularConserved SequenceDimerizationEscherichia coliGammaproteobacteriaGene ExpressionGenetic Complementation TestGeobacillus stearothermophilusMutagenesis, Site-DirectedRNA, TransferSequence Homology, Amino AcidStructure-Activity RelationshipTyrosineTyrosine-tRNA LigaseConceptsBacterial tyrosyl-tRNA synthetasesBacterial tyrosyl tRNA synthetaseConserved amino acidsAmino acidsAmino acid identityAmino-terminal regionActive site domainCarboxy-terminal segmentTyrosyl-tRNA synthetasesTyrosyl-tRNA synthetaseAcid identityLargest subfamilyCarboxy terminusSite domainTRNA bindingEnzyme functionTyr-AMPTRNATyrRSResiduesEquivalent roleBindingH306S356K395
2000
A Mutant Escherichia coli Tyrosyl-tRNA Synthetase Utilizes the Unnatural Amino Acid Azatyrosine More Efficiently than Tyrosine*
Hamano-Takaku F, Iwama T, Saito-Yano S, Takaku K, Monden Y, Kitabatake M, Söll D, Nishimura S. A Mutant Escherichia coli Tyrosyl-tRNA Synthetase Utilizes the Unnatural Amino Acid Azatyrosine More Efficiently than Tyrosine*. Journal Of Biological Chemistry 2000, 275: 40324-40328. PMID: 11006270, DOI: 10.1074/jbc.m003696200.Peer-Reviewed Original ResearchConceptsUnnatural amino acidsTyrosyl-tRNA synthetaseEscherichia coli tyrosyl-tRNA synthetasePosition 130Amino acidsVivo protein biosynthesisE. coli cellsAminoacyl-tRNA formationSingle point mutationTyrRS mutantsCellular proteinsProtein biosynthesisTYR geneMutant enzymesPlasmid libraryReplacement of phenylalanineColi cellsImmense potentialNormal phenotypeEfficient productionPoint mutationsTyrRSProteinPolymerase chain reaction techniqueSynthetaseAncient Adaptation of the Active Site of Tryptophanyl-tRNA Synthetase for Tryptophan Binding †
Ibba M, Stange-Thomann N, Kitabatake M, Ali K, Söll I, Carter, C, Michael Ibba, and, Söll D. Ancient Adaptation of the Active Site of Tryptophanyl-tRNA Synthetase for Tryptophan Binding †. Biochemistry 2000, 39: 13136-13143. PMID: 11052665, DOI: 10.1021/bi001512t.Peer-Reviewed Original ResearchMeSH KeywordsAcylationAnimalsBacillus subtilisBacterial ProteinsBinding SitesCattleDiphosphatesDNA Mutational AnalysisDNA, BacterialEvolution, MolecularGeobacillus stearothermophilusHumansKineticsMiceMutagenesis, Site-DirectedProtein BindingRabbitsRNA, Transfer, TrpSequence Homology, Amino AcidTryptophanTryptophan-tRNA LigaseTyrosineConceptsAmino acid specificityActive site residuesTyrosyl-tRNA synthetasesTryptophanyl-tRNA synthetaseAncient adaptationAnalogous residuesGlu side chainsTryptophan replacementHomologous positionsSystematic mutationAromatic side chainsTrpRSTryptophan recognitionBacillus stearothermophilusSide chainsTryptophan bindingTyrRSResiduesCommon originCompetitive inhibitorMutationsTrp bindingMechanistic supportCatalytic efficiencyActive site