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Nucleic Acids Research Advance Access originally published online on February 7, 2008
Nucleic Acids Research 2008 36(5):1713-1722; doi:10.1093/nar/gkn014
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Nucleic Acids Research, 2008, Vol. 36, No. 5 1713-1722
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Interaction of p21CDKN1A with PCNA regulates the histone acetyltransferase activity of p300 in nucleotide excision repair

Ornella Cazzalini1, Paola Perucca1, Monica Savio1, Daniela Necchi1,2, Livia Bianchi1, Lucia A. Stivala1, Bernard Ducommun3, A. Ivana Scovassi4 and Ennio Prosperi2,4,*

1Dipartimento di Medicina Sperimentale, sez. Patologia Generale "C. Golgi", Università di Pavia, 27100 Pavia, 2Dipartimento di Biologia Animale, Università di Pavia, 27100 Pavia, Italy, 3LBCMCP, CNRS UMR5088, Université P. Sabatier, 31062 Toulouse, France and 4Istituto di Genetica Molecolare del CNR, 27100 Pavia, Italy

*To whom correspondence should be addressed. Tel: +39 0382 986267; Fax: +39 0382 986430; Email: prosperi{at}igm.cnr.it

Received July 24, 2007. Revised January 8, 2008. Accepted January 9, 2008.

The cell-cycle inhibitor p21CDKN1A has been suggested to directly participate in DNA repair, thanks to the interaction with PCNA. Yet, its role has remained unclear. Among proteins interacting with both p21 and PCNA, the histone acetyltransferase (HAT) p300 has been shown to participate in DNA repair. Here we report evidence indicating that p21 protein localizes and interacts with both p300 and PCNA at UV-induced DNA damage sites. The interaction between p300 and PCNA is regulated in vivo by p21. Indeed, loss of p21, or its inability to bind PCNA, results in a prolonged binding to chromatin and an increased association of p300 with PCNA, in UV-irradiated cells. Concomitantly, HAT activity of p300 is reduced after DNA damage. In vitro experiments show that inhibition of p300 HAT activity induced by PCNA is relieved by p21, which disrupts the association between recombinant p300 and PCNA. These results indicate that p21 is required during DNA repair to regulate p300 HAT activity by disrupting its interaction with PCNA.


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