E2F family members are differentially regulated by reversible acetylation.

G Marzio; C Wagener; M I Gutierrez; P Cartwright; K Helin; M Giacca

E2F family members are differentially regulated by reversible acetylation.

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

181 Citations (Scopus)

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.

Original language	English
Journal	Journal of Biological Chemistry
Volume	275
Issue number	15
Pages (from-to)	10887-92
Number of pages	5
ISSN	0021-9258
Publication status	Published - 2000

Cite this

@article{8983409053d611dd8d9f000ea68e967b,

title = "E2F family members are differentially regulated by reversible acetylation.",

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.",

author = "G Marzio and C Wagener and Gutierrez, {M I} and P Cartwright and K Helin and M Giacca",

note = "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",

year = "2000",

language = "English",

volume = "275",

pages = "10887--92",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology, Inc.",

number = "15",

}

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 -

E2F family members are differentially regulated by reversible acetylation.

Abstract

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