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. 2000 Apr 14;275(15):10887-92.
doi: 10.1074/jbc.275.15.10887.

E2F family members are differentially regulated by reversible acetylation

G Marzio  1 , C Wagener, M I Gutierrez, P Cartwright, K Helin, M Giacca
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Free article

E2F family members are differentially regulated by reversible acetylation

G Marzio et al. J Biol Chem. .
Free article

Abstract

The six members of the E2F family of transcription factors play a key role in the control of cell cycle progression by regulating the expression of genes involved in DNA replication and cell proliferation. E2F-1, -2, and -3 belong to a structural and functional subfamily distinct from those of the other E2F family members. Here we report that E2F-1, -2, and -3, but not E2F-4, -5, and -6, associate with and are acetylated by p300 and cAMP-response element-binding protein acetyltransferases. Acetylation occurs at three conserved lysine residues located at the N-terminal boundary of their DNA binding domains. Acetylation of E2F-1 in vitro and in vivo markedly increases its binding affinity for a consensus E2F DNA-binding site, which is paralleled by enhanced transactivation of an E2F-responsive promoter. Acetylation of E2F-1 can be reversed by histone deacetylase-1, indicating that reversible acetylation is a mechanism for regulation also of non-histone proteins.

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