Mechanisms of P/CAF auto-acetylation.

P/CAF is a histone acetyltransferase enzyme which was originally identified as a CBP/p300-binding protein. In this manuscript we report that human P/CAF is acetylated in vivo. We find that P/CAF is acetylated by itself and by p300 but not by CBP. P/CAF acetylation can be an intra- or intermolecular event. ...
The intermolecular acetylation requires the N-terminal domain of P/CAF. The intramolecular acetylation targets five lysines (416-442) at the P/CAF C-terminus, which are in the nuclear localisation signal (NLS). Finally, we show that acetylation of P/CAF leads to an increment of its histone acetyltransferase (HAT) activity. These findings identify a new post-translation modification on P/CAF which may regulate its function.
Mesh Terms:
Acetylation, Acetyltransferases, Cell Cycle Proteins, Cell Line, Histone Acetyltransferases, Humans, Nuclear Localization Signals, Nuclear Proteins, Protein Structure, Tertiary, Saccharomyces cerevisiae Proteins, Trans-Activators, Transcription Factors, p300-CBP Transcription Factors
Nucleic Acids Res.
Date: Aug. 01, 2003
Download Curated Data For This Publication
170070
Switch View:
  • Interactions 3