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