Mechanisms of P/CAF auto-acetylation

作者：Santos Rosa H; Valls E; Kouzarides T; Martinez Balbas M^*

来源：Nucleic Acids Research, 2003, 31(15): 4285-4292.

DOI：10.1093/nar/gkg655

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.

• 出版日期2003-8-1