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A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
X J Yang1, V V Ogryzko, J Nishikawa
1Laboratory of Molecular Growth Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892-2753, USA.
Nature
|July 25, 1996
Summary
A newly discovered factor, P/CAF, inhibits cell cycle progression by competing with the adenoviral oncoprotein E1A. This finding reveals a new mechanism for controlling cell growth and E1A
Area of Science:
- Molecular Biology
- Cell Biology
- Virology
Background:
- The adenoviral oncoprotein E1A drives cell cycle progression.
- E1A interacts with p300/CBP and retinoblastoma proteins.
- Dysregulation of cell cycle control is a hallmark of viral oncogenesis.
Purpose of the Study:
- To identify cellular factors that antagonize E1A.
- To investigate the role of histone acetyltransferases in E1A-mediated cell cycle control.
- To understand the mechanism by which P/CAF affects cell proliferation.
Main Methods:
- Co-immunoprecipitation assays to study protein interactions.
- Expression of P/CAF in HeLa cells.
- Cell cycle analysis (e.g., flow cytometry).
- Histone acetylase activity assays.
Main Results:
- A novel p300/CBP-associated factor (P/CAF) with histone acetylase activity was identified.
- P/CAF competes with E1A for binding to p300/CBP.
- Overexpression of P/CAF inhibits cell-cycle progression in HeLa cells.
- P/CAF counteracts the mitogenic effects of E1A.
- E1A disrupts the interaction between p300/CBP and its associated histone acetylase.
Conclusions:
- P/CAF acts as a cellular antagonist to the adenoviral oncoprotein E1A.
- P/CAF's histone acetylase activity is crucial for its anti-proliferative effects.
- E1A's oncogenic activity involves interfering with normal histone acetylation pathways.