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Acetylation of adenovirus E1A regulates binding of the transcriptional corepressor CtBP

Q Zhang1, H Yao, N Vo

  • 1Vollum Institute, Oregon Health Sciences University, Portland, OR 97201, USA.

Proceedings of the National Academy of Sciences of the United States of America
|December 13, 2000
PubMed

Insights

Adenovirus E1A protein acetylation, specifically at Lys-239, disrupts its binding to CtBP. This acetylation by histone acetyltransferases may be a general mechanism for gene activation by releasing repressor complexes.

Area of Science:

  • Molecular Biology
  • Virology
  • Epigenetics

Background:

  • Adenovirus E1A protein regulates cellular processes by interacting with key cellular proteins.
  • E1A's N-terminus binds CBP/p300 and histone acetyltransferases, while its C-terminus binds CtBP, a protein associated with histone deacetylases.

Purpose of the Study:

  • To investigate the role of E1A acetylation in its interaction with CtBP.
  • To identify specific acetylation sites on E1A and their functional consequences.

Main Methods:

  • In vitro and in vivo binding assays to study E1A-CtBP interactions.
  • Site-directed mutagenesis to alter Lys-239 residue on E1A.
  • Peptide competition assays and reporter gene assays to assess functional impact.
  • Development of an antibody specific for acetylated Lys-239 E1A.

Main Results:

  • 12S E1A can be acetylated by p300 and P/CAF, with Lys-239 identified as an acetylation site.
  • Mutation of Lys-239 to Gln or Ala abolished CtBP binding in vitro and disrupted the E1A-CtBP interaction in vivo.
  • Acetylation of Lys-239 blocked E1A-CtBP interaction, and mutation of Lys-239 decreased E1A's ability to inhibit CREB-stimulated gene expression.
  • Lys-239 acetylation was confirmed in cells using a specific antibody.

Conclusions:

  • Acetylation of Adenovirus E1A at Lys-239 is a critical regulatory mechanism that disrupts its interaction with CtBP.
  • This acetylation event, mediated by histone acetyltransferases, may represent a general strategy for transcriptional activation by releasing repressor complexes.
  • The findings provide insights into the epigenetic regulation of viral gene expression and cellular transformation.

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