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http://purl.uniprot.org/citations/10918062http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10918062http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10918062http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/10918062http://www.w3.org/2000/01/rdf-schema#comment"In Escherichia coli, tyrosyl-tRNA synthetase is known to esterify tRNA(Tyr) with tyrosine. Resulting d-Tyr-tRNA(Tyr) can be hydrolyzed by a d-Tyr-tRNA(Tyr) deacylase. By monitoring E. coli growth in liquid medium, we systematically searched for other d-amino acids, the toxicity of which might be exacerbated by the inactivation of the gene encoding d-Tyr-tRNA(Tyr) deacylase. In addition to the already documented case of d-tyrosine, positive responses were obtained with d-tryptophan, d-aspartate, d-serine, and d-glutamine. In agreement with this observation, production of d-Asp-tRNA(Asp) and d-Trp-tRNA(Trp) by aspartyl-tRNA synthetase and tryptophanyl-tRNA synthetase, respectively, was established in vitro. Furthermore, the two d-aminoacylated tRNAs behaved as substrates of purified E. coli d-Tyr-tRNA(Tyr) deacylase. These results indicate that an unexpected high number of d-amino acids can impair the bacterium growth through the accumulation of d-aminoacyl-tRNA molecules and that d-Tyr-tRNA(Tyr) deacylase has a specificity broad enough to recycle any of these molecules. The same strategy of screening was applied using Saccharomyces cerevisiae, the tyrosyl-tRNA synthetase of which also produces d-Tyr-tRNA(Tyr), and which, like E. coli, possesses a d-Tyr-tRNA(Tyr) deacylase activity. In this case, inhibition of growth by the various 19 d-amino acids was followed on solid medium. Two isogenic strains containing or not the deacylase were compared. Toxic effects of d-tyrosine and d-leucine were reinforced upon deprivation of the deacylase. This observation suggests that, in yeast, at least two d-amino acids succeed in being transferred onto tRNAs and that, like in E. coli, the resulting two d-aminoacyl-tRNAs are substrates of a same d-aminoacyl-tRNA deacylase."xsd:string
http://purl.uniprot.org/citations/10918062http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m005166200"xsd:string
http://purl.uniprot.org/citations/10918062http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m005166200"xsd:string
http://purl.uniprot.org/citations/10918062http://purl.uniprot.org/core/author"Blanquet S."xsd:string
http://purl.uniprot.org/citations/10918062http://purl.uniprot.org/core/author"Blanquet S."xsd:string
http://purl.uniprot.org/citations/10918062http://purl.uniprot.org/core/author"Plateau P."xsd:string
http://purl.uniprot.org/citations/10918062http://purl.uniprot.org/core/author"Plateau P."xsd:string
http://purl.uniprot.org/citations/10918062http://purl.uniprot.org/core/author"Soutourina J."xsd:string
http://purl.uniprot.org/citations/10918062http://purl.uniprot.org/core/author"Soutourina J."xsd:string
http://purl.uniprot.org/citations/10918062http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10918062http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10918062http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10918062http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10918062http://purl.uniprot.org/core/pages"32535-32542"xsd:string
http://purl.uniprot.org/citations/10918062http://purl.uniprot.org/core/pages"32535-32542"xsd:string
http://purl.uniprot.org/citations/10918062http://purl.uniprot.org/core/title"Metabolism of D-aminoacyl-tRNAs in Escherichia coli and Saccharomyces cerevisiae cells."xsd:string
http://purl.uniprot.org/citations/10918062http://purl.uniprot.org/core/title"Metabolism of D-aminoacyl-tRNAs in Escherichia coli and Saccharomyces cerevisiae cells."xsd:string
http://purl.uniprot.org/citations/10918062http://purl.uniprot.org/core/volume"275"xsd:string
http://purl.uniprot.org/citations/10918062http://purl.uniprot.org/core/volume"275"xsd:string
http://purl.uniprot.org/citations/10918062http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10918062
http://purl.uniprot.org/citations/10918062http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10918062
http://purl.uniprot.org/citations/10918062http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10918062