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http://purl.uniprot.org/citations/1924298http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1924298http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1924298http://www.w3.org/2000/01/rdf-schema#comment"Phenylalanyl-tRNA synthetases [L-phenylalanine:tRNAPhe ligase (AMP-forming), EC 6.1.1.20] from Escherichia coli, yeast cytoplasm, and mammalian cytoplasm have an unusual conserved alpha 2 beta 2 quaternary structure that is shared by only one other aminoacyl-tRNA synthetase. Both subunits are required for activity. We show here that a single mitochondrial polypeptide from Saccharomyces cerevisiae is an active phenylalanyl-tRNA synthetase. This protein (the MSF1 gene product) is active as a monomer. It has all three characteristic sequence motifs of the class II aminoacyl-tRNA synthetases, and its activity may result from the recruitment of additional sequences into an alpha-subunit-like structure."xsd:string
http://purl.uniprot.org/citations/1924298http://purl.org/dc/terms/identifier"doi:10.1073/pnas.88.19.8387"xsd:string
http://purl.uniprot.org/citations/1924298http://purl.org/dc/terms/identifier"doi:10.1073/pnas.88.19.8387"xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/author"Walter P."xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/author"Walter P."xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/author"Fasiolo F."xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/author"Fasiolo F."xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/author"Boulanger Y."xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/author"Boulanger Y."xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/author"Sanni A."xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/author"Sanni A."xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/author"Ebel J.-P."xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/author"Ebel J.-P."xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/pages"8387-8391"xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/pages"8387-8391"xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/title"Evolution of aminoacyl-tRNA synthetase quaternary structure and activity: Saccharomyces cerevisiae mitochondrial phenylalanyl-tRNA synthetase."xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/title"Evolution of aminoacyl-tRNA synthetase quaternary structure and activity: Saccharomyces cerevisiae mitochondrial phenylalanyl-tRNA synthetase."xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/volume"88"xsd:string
http://purl.uniprot.org/citations/1924298http://purl.uniprot.org/core/volume"88"xsd:string