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Cell cycle-dependent recruitment of HDAC-1 correlates with deacetylation of histone H4 on an Rb-E2F target promoter

R Ferreira1, I Naguibneva, M Mathieu

  • 1Laboratoire 'Oncogenèse, Différenciation et Transduction du Signal', CNRS UPR 9079, Institut Fédératif André Lwoff, 7 rue Guy Moquet, 94801 Villejuif, France.

EMBO Reports
|August 25, 2001
PubMed

Insights

Histone deacetylase 1 (HDAC-1) binds E2F target promoters during early G1 in proliferating cells, repressing cell proliferation. HDAC-1 is released at the G1-S transition, correlating with increased histone acetylation.

Area of Science:

  • Molecular Biology
  • Cell Cycle Regulation
  • Epigenetics

Background:

  • The transcription factor E2F controls cell proliferation and is repressed by pocket proteins during growth arrest and early G1.
  • Class I histone deacetylases (HDACs) are implicated in E2F repression by pocket proteins.
  • It is hypothesized that HDACs are recruited to E2F target promoters to deacetylate histones.

Purpose of the Study:

  • To directly test the hypothesis that HDACs are recruited to E2F target promoters.
  • To investigate the role of HDAC-1 in E2F-mediated repression during the cell cycle.

Main Methods:

  • Formaldehyde cross-linked chromatin immunoprecipitation (XChIP) assays were used.
  • HDAC association with an E2F target promoter was evaluated in living cells.

Main Results:

  • HDAC-1 was found to be stably bound to an E2F target promoter during early G1 in proliferating cells.
  • HDAC-1 was released from the promoter at the G1-S transition.
  • An inverse correlation was observed between HDAC-1 recruitment and histone H4 acetylation on specific lysines.

Conclusions:

  • HDAC-1 is recruited to E2F target promoters during early G1, contributing to cell cycle control.
  • HDAC-1 binding and histone deacetylation are dynamically regulated during the G1-S transition.
  • These findings provide direct evidence for the role of HDAC-1 in regulating E2F activity and cell proliferation.

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