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 techniqueSynthetase
1968
Studies on polynucleotides LXXXV. Partial purification of an amber supressor tRNA and studies on in vitro suppression
Söll D. Studies on polynucleotides LXXXV. Partial purification of an amber supressor tRNA and studies on in vitro suppression. Journal Of Molecular Biology 1968, 34: 175-187. PMID: 4938541, DOI: 10.1016/0022-2836(68)90243-x.Peer-Reviewed Original ResearchConceptsSuppressor tRNAColi cellsAmber suppressor genesAmber suppressor tRNAProtein synthesis experimentsEscherichia coli cellsE. coli cellsAmber mutantsTRNASuppressor geneProtein synthesisCrude tRNAGenesRNAPartial purificationBacteriophage f2CellsMutantsRibosomesUAGSpeciesMessengerSuppressionChain terminationBinding