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Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/124638
Título

Regulation of E2F1 activity by acetylation

AutorMartínez-Balbás, Marian ; Bauer, Uta Maria; Nielsen, Soren Jensby; Brehm, Alexander; Kouzarides, Tony
Palabras claveAcetylation
E2F1
Histone deacetylase
P/CAF
p300
Retinoblastoma protein
Fecha de publicación15-feb-2000
EditorEuropean Molecular Biology Organization
CitaciónEMBO Journal 19(4): 662-671 (2000)
ResumenDuring the G1 phase of the cell cycle, an E2F-RB complex represses transcription, via the recruitment of histone deacetylase activity. Phosphorylation of RB at the G1/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
Versión del editorhttp://dx.doi.org/10.1093/emboj/19.4.662
URIhttp://hdl.handle.net/10261/124638
DOI10.1093/emboj/19.4.662
ISSN0261-4189
E-ISSN1460-2075
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