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A mechanism of COOH-terminal binding protein-mediated repression

Alison R Meloni1, Chun-Hsiang Lai, Tso-Pang Yao

  • 1Department of Molecular Genetics and Microbiology, Duke University Medical Center, Box 3054, Durham, North Carolina 27710, USA.

Molecular Cancer Research : MCR
|October 29, 2005
PubMed

Insights

The E2F4/p130 complex represses gene transcription via two pathways. One pathway involves the COOH-terminal binding protein (CtBP) corepressor inhibiting histone acetylation, controlling gene expression in quiescent cells.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Epigenetics

Background:

  • E2F4 and E2F5 proteins associate with p130 in quiescent cells.
  • This complex represses transcription of cell growth-related genes.
  • Rb-mediated repression involves both HDAC-dependent and HDAC-independent mechanisms.

Purpose of the Study:

  • Investigate HDAC-independent repression mechanisms.
  • Elucidate the role of COOH-terminal binding protein (CtBP) in E2F/p130-mediated repression.
  • Determine how CtBP influences histone acetylation.

Main Methods:

  • Co-immunoprecipitation assays to study protein interactions.
  • In vitro assays to assess histone acetyltransferase activity.
  • Analysis of CtBP functional domains required for repression.

Main Results:

  • CtBP interacts with p130, mediating HDAC-independent repression.
  • CtBP inhibits the histone acetyltransferase activity of CREB-binding protein.
  • A specific NH2-terminal region of CtBP is crucial for both repression and inhibition of acetylation.

Conclusions:

  • E2F/p130-mediated repression involves two complementary mechanisms.
  • Both mechanisms converge on the control of histone acetylation at target gene promoters.
  • CtBP plays a key role in regulating histone acetylation during transcriptional repression.

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