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Originally published In Press as doi:10.1074/jbc.M100934200 on February 14, 2001

J. Biol. Chem., Vol. 276, Issue 20, 16804-16809, May 18, 2001
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p300-mediated Acetylation of Human Transcriptional Coactivator PC4 Is Inhibited by Phosphorylation*

B. R. Prashanth Kumar, V. SwaminathanDagger , Sourav Banerjee, and Tapas K. Kundu§

From the Transcription and Disease Laboratory, Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur, Bangalore-560 064, India

The human positive coactivator 4 (PC4) acts as a general coactivator for activator-dependent transcription, the activity of which is regulated negatively by phosphorylation. We report here that PC4 can be acetylated specifically by another coactivator, p300. Interestingly, phosphorylation of PC4 by casein kinase II inhibits the p300-mediated acetylation. Mass spectral analysis revealed that there are at least two lysine residues acetylated in PC4, as a result of which its DNA binding activity is stimulated.

* This work was supported in part by Jawaharlal Nehru Center for Advanced Scientific Research and the Council of Scientific and Industrial Research.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Council of Scientific and Industrial Research Junior Research Fellow.

§ To whom correspondence should be addressed. Tel.: 91-80-8462750 (Ext. 257); Fax: 91-80-8462766; E-mail: tapas@jncasr.ac.in.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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