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http://purl.uniprot.org/citations/20444689http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20444689http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20444689http://www.w3.org/2000/01/rdf-schema#comment"Lysine methylation is one of the most common protein modifications. Although lysine methylation of histones has been extensively studied and linked to gene regulation, that of non-histone proteins remains incompletely understood. Here, we show a novel regulatory role of ribosomal protein methylation. Using an in vitro methyltransferase assay, we found that Schizosaccharomyces pombe Set13, a SET domain protein encoded by SPAC688.14, specifically methylates lysine 55 of ribosomal protein L42 (Rpl42). Mass spectrometric analysis revealed that endogenous Rpl42 is monomethylated at lysine 55 in wild-type S. pombe cells and that the methylation is lost in Delta set13 mutant cells. Delta set13 and Rpl42 methylation-deficient mutant S. pombe cells showed higher cycloheximide sensitivity and defects in stress-responsive growth control compared with wild type. Genetic analyses suggested that the abnormal growth phenotype was distinct from the conserved stress-responsive pathway that modulates translation initiation. Furthermore, the Rpl42 methylation-deficient mutant cells showed a reduced ability to survive after entering stationary phase. These results suggest that Rpl42 methylation plays direct roles in ribosomal function and cell proliferation control independently of the general stress-response pathway."xsd:string
http://purl.uniprot.org/citations/20444689http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.132274"xsd:string
http://purl.uniprot.org/citations/20444689http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.132274"xsd:string
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/author"Nakayama J."xsd:string
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/author"Nakayama J."xsd:string
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/author"Shirai A."xsd:string
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/author"Shirai A."xsd:string
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/author"Shinmyozu K."xsd:string
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/author"Shinmyozu K."xsd:string
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/author"Sadaie M."xsd:string
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/author"Sadaie M."xsd:string
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/pages"22448-22460"xsd:string
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/pages"22448-22460"xsd:string
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/title"Methylation of ribosomal protein L42 regulates ribosomal function and stress-adapted cell growth."xsd:string
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/title"Methylation of ribosomal protein L42 regulates ribosomal function and stress-adapted cell growth."xsd:string
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/volume"285"xsd:string
http://purl.uniprot.org/citations/20444689http://purl.uniprot.org/core/volume"285"xsd:string
http://purl.uniprot.org/citations/20444689http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20444689
http://purl.uniprot.org/citations/20444689http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20444689