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Nucleic Acids Res. 2003 Aug 1;31(15):4285-92.

Mechanisms of P/CAF auto-acetylation.

Author information

1
Instituto de Biología Molecular de Barcelona, CID, Consejo Superior de Investigaciones Científicas (CSIC), Jordi Girona 18-26, E-08034 Barcelona, Spain.

Abstract

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.

PMID:
12888487
PMCID:
PMC169960
DOI:
10.1093/nar/gkg655
[Indexed for MEDLINE]
Free PMC Article

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