TY - JOUR
T1 - E2F family members are differentially regulated by reversible acetylation.
AU - Marzio, G
AU - Wagener, C
AU - Gutierrez, M I
AU - Cartwright, P
AU - Helin, K
AU - Giacca, M
N1 - Keywords: Acetylation; Acetyltransferases; Carrier Proteins; Cell Cycle Proteins; Cyclic AMP Response Element-Binding Protein; DNA; DNA-Binding Proteins; E2F Transcription Factors; E2F1 Transcription Factor; Histone Acetyltransferases; Histone Deacetylases; Saccharomyces cerevisiae Proteins; Trans-Activation (Genetics); Transcription Factors
PY - 2000
Y1 - 2000
N2 - 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.
AB - 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.
M3 - Journal article
C2 - 10753885
SN - 0021-9258
VL - 275
SP - 10887
EP - 10892
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 15
ER -