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http://purl.uniprot.org/citations/28126738http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28126738http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28126738http://www.w3.org/2000/01/rdf-schema#comment"We have previously characterised the histone lysine methyltransferase properties of PRDM9, a member of the PRDM family of putative transcriptional regulators. PRDM9 displays broad substrate recognition and methylates a range of histone substrates, including octamers, core histone proteins, and peptides. In the present study, we show that PRDM9 performs intramolecular automethylation on multiple lysine residues localised to a lysine-rich region on the post-SET (suppressor of variegation 3-9, enhancer of zeste and trithorax) domain. PRDM9 automethylation is abolished by a single active-site mutation, C321P, also known to disrupt interactions with S-adenosylmethionine. We have taken an initial step towards tool compound generation through rational design of a substrate-mimic, peptidic inhibitor of PRDM9 automethylation. The discovery of automethylation in PRDM9 adds a new dimension to our understanding of PRDM9 enzymology."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.org/dc/terms/identifier"doi:10.1042/bcj20161067"xsd:string
http://purl.uniprot.org/citations/28126738http://purl.org/dc/terms/identifier"doi:10.1042/bcj20161067"xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Hill J."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Hill J."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Li R."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Li R."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Peng J."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Peng J."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Wu L."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Wu L."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Joy J."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Joy J."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Guccione E."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Guccione E."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Wee J.L."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Wee J.L."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Chew S.Y."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Chew S.Y."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Koh-Stenta X."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Koh-Stenta X."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Kwek P.Z."xsd:string
http://purl.uniprot.org/citations/28126738http://purl.uniprot.org/core/author"Kwek P.Z."xsd:string