A p300/CBP-associated Factor That Competes With the Adenoviral Oncoprotein E1A

Nature. 1996 Jul 25;382(6589):319-24. doi: 10.1038/382319a0.

Abstract

The adenoviral oncoprotein E1A induces progression through the cell cycle by binding to the products of the p300/CBP and retinoblastoma gene families. A new cellular p300/CBP-associated factor (P/CAF) having intrinsic histone acetylase activity has been identified that competes with E1A. Exogenous expression of P/CAF in HeLa cells inhibits cell-cycle progression and counteracts the mitogenic activity of E1A. E1A disturbs the normal cellular interaction between p300/CBP and its associated histone acetylase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetyltransferases / genetics
  • Acetyltransferases / metabolism
  • Adenovirus E1A Proteins / metabolism*
  • Amino Acid Sequence
  • Binding, Competitive
  • Cell Cycle
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism*
  • Cloning, Molecular
  • Escherichia coli
  • HeLa Cells
  • Histone Acetyltransferases
  • Humans
  • Molecular Sequence Data
  • Nuclear Proteins / metabolism*
  • Protein Binding
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Saccharomyces cerevisiae Proteins*
  • Sequence Deletion
  • Trans-Activators*
  • Transcription Factors / metabolism*
  • p300-CBP Transcription Factors

Substances

  • Adenovirus E1A Proteins
  • Cell Cycle Proteins
  • Nuclear Proteins
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae Proteins
  • Trans-Activators
  • Transcription Factors
  • Acetyltransferases
  • Histone Acetyltransferases
  • p300-CBP Transcription Factors
  • p300-CBP-associated factor

Associated data

  • GENBANK/U57316
  • GENBANK/U57317