Nucleic Acids Research, 2003, Vol. 31, No. 15 4285-4292
© 2003 Oxford University Press
Mechanisms of P/CAF auto-acetylation
Wellcome/CRC Institute and Department of Pathology, Cambridge University, Tennis Court Road, Cambridge, CBN2 1QR, UK and 1 Instituto de Biología Molecular de Barcelona, CID, Consejo Superior de Investigaciones Científicas (CSIC), Jordi Girona 18–26, E-08034 Barcelona, Spain
*To whom correspondence should be addressed. Tel: +34 93 4006141; Fax: +34 93 2045904; Email: mmbbmc{at}ibmb.csic.es
Correspondence may also be addressed to Tony Kouzarides. Tel: +44 1223 334112; Fax: +44 1223 334089; Email: tk106{at}mole.bio.cam.ac.uk
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.
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