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http://purl.uniprot.org/citations/10675335http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10675335http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10675335http://www.w3.org/2000/01/rdf-schema#comment"During the G(1) phase of the cell cycle, an E2F-RB complex represses transcription, via the recruitment of histone deacetylase activity. Phosphorylation of RB at the G(1)/S boundary generates a pool of 'free' E2F, which then stimulates transcription of S-phase genes. Given that E2F1 activity is stimulated by p300/CBP acetylase and repressed by an RB-associated deacetylase, we asked if E2F1 was subject to modification by acetylation. We show that the p300/CBP-associated factor P/CAF, and to a lesser extent p300/CBP itself, can acetylate E2F1 in vitro and that intracellular E2F1 is acetylated. The acetylation sites lie adjacent to the E2F1 DNA-binding domain and involve lysine residues highly conserved in E2F1, 2 and 3. Acetylation by P/CAF has three functional consequences on E2F1 activity: increased DNA-binding ability, activation potential and protein half-life. These results suggest that acetylation stimulates the functions of the non-RB bound 'free' form of E2F1. Consistent with this, we find that the RB-associated histone deacetylase can deacetylate E2F1. These results identify acetylation as a novel regulatory modification that stimulates E2F1's activation functions."xsd:string
http://purl.uniprot.org/citations/10675335http://purl.org/dc/terms/identifier"doi:10.1093/emboj/19.4.662"xsd:string
http://purl.uniprot.org/citations/10675335http://purl.org/dc/terms/identifier"doi:10.1093/emboj/19.4.662"xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/author"Kouzarides T."xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/author"Kouzarides T."xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/author"Martinez-Balbas M.A."xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/author"Martinez-Balbas M.A."xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/author"Bauer U.M."xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/author"Bauer U.M."xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/author"Brehm A."xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/author"Brehm A."xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/author"Nielsen S.J."xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/author"Nielsen S.J."xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/pages"662-671"xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/pages"662-671"xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/title"Regulation of E2F1 activity by acetylation."xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/title"Regulation of E2F1 activity by acetylation."xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/10675335http://purl.uniprot.org/core/volume"19"xsd:string