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http://purl.uniprot.org/citations/27226603http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27226603http://www.w3.org/2000/01/rdf-schema#comment"Non-protein amino acids, particularly isomers of the proteinogenic amino acids, present a threat to proteome integrity if they are mistakenly inserted into proteins. Quality control during aminoacyl-tRNA synthesis reduces non-protein amino acid incorporation by both substrate discrimination and proofreading. For example phenylalanyl-tRNA synthetase (PheRS) proofreads the non-protein hydroxylated phenylalanine derivative m-Tyr after its attachment to tRNA(Phe) We now show in Saccharomyces cerevisiae that PheRS misacylation of tRNA(Phe) with the more abundant Phe oxidation product o-Tyr is limited by kinetic discrimination against o-Tyr-AMP in the transfer step followed by o-Tyr-AMP release from the synthetic active site. This selective rejection of a non-protein aminoacyl-adenylate is in addition to known kinetic discrimination against certain non-cognates in the activation step as well as catalytic hydrolysis of mispaired aminoacyl-tRNA(Phe) species. We also report an unexpected resistance to cytotoxicity by a S. cerevisiae mutant with ablated post-transfer editing activity when supplemented with o-Tyr, cognate Phe, or Ala, the latter of which is not a substrate for activation by this enzyme. Our phenotypic, metabolomic, and kinetic analyses indicate at least three modes of discrimination against non-protein amino acids by S. cerevisiae PheRS and support a non-canonical role for SccytoPheRS post-transfer editing in response to amino acid stress."xsd:string
http://purl.uniprot.org/citations/27226603http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m116.726828"xsd:string
http://purl.uniprot.org/citations/27226603http://purl.uniprot.org/core/author"Ibba M."xsd:string
http://purl.uniprot.org/citations/27226603http://purl.uniprot.org/core/author"Hwang L."xsd:string
http://purl.uniprot.org/citations/27226603http://purl.uniprot.org/core/author"Faull K."xsd:string
http://purl.uniprot.org/citations/27226603http://purl.uniprot.org/core/author"Moghal A."xsd:string
http://purl.uniprot.org/citations/27226603http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27226603http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/27226603http://purl.uniprot.org/core/pages"15796-15805"xsd:string
http://purl.uniprot.org/citations/27226603http://purl.uniprot.org/core/title"Multiple Quality Control Pathways Limit Non-protein Amino Acid Use by Yeast Cytoplasmic Phenylalanyl-tRNA Synthetase."xsd:string
http://purl.uniprot.org/citations/27226603http://purl.uniprot.org/core/volume"291"xsd:string
http://purl.uniprot.org/citations/27226603http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27226603
http://purl.uniprot.org/citations/27226603http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27226603
http://purl.uniprot.org/uniprot/P15625#attribution-08BC4C02E2527801DB5E903EA8D88144http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/27226603
http://purl.uniprot.org/uniprot/#_P15625-mappedCitation-27226603http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27226603
http://purl.uniprot.org/uniprot/P15625http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/27226603