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Mol Cell Biol, June 1998, p. 3563-3571, Vol. 18, No. 6
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

XRCC1 Is Specifically Associated with Poly(ADP-Ribose) Polymerase and Negatively Regulates Its Activity following DNA Damage

Murielle Masson,1 Claude Niedergang,1 Valérie Schreiber,1 Sylviane Muller,2 Josiane Menissier-de Murcia,1 and Gilbert de Murcia1,*

UPR 9003 du Centre National de la Recherche Scientifique, Cancérogenèse et Mutagenèse Moléculaire et Structurale, Ecole Supérieure de Biotechnologie de Strasbourg, 67400 Illkirch-Graffenstaden,1 and UPR 9021 du Centre National de la Recherche Scientifique, Immunochimie des Peptides et des Virus, Institut de Biologie Moléculaire et Cellulaire, 67000 Strasbourg,2 France

Received 4 September 1997/Returned for modification 13 October 1997/Accepted 6 March 1998

Poly(ADP-ribose) polymerase (PARP; EC 2.4.2.30) is a zinc-finger DNA-binding protein that detects and signals DNA strand breaks generated directly or indirectly by genotoxic agents. In response to these breaks, the immediate poly(ADP-ribosyl)ation of nuclear proteins involved in chromatin architecture and DNA metabolism converts DNA damage into intracellular signals that can activate DNA repair programs or cell death options. To have greater insight into the physiological function of this enzyme, we have used the two-hybrid system to find genes encoding proteins putatively interacting with PARP. We have identified a physical association between PARP and the base excision repair (BER) protein XRCC1 (X-ray repair cross-complementing 1) in the Saccharomyces cerevisiae system, which was further confirmed to exist in mammalian cells. XRCC1 interacts with PARP by its central region (amino acids 301 to 402), which contains a BRCT (BRCA1 C terminus) module, a widespread motif in DNA repair and DNA damage-responsive cell cycle checkpoint proteins. Overexpression of XRCC1 in Cos-7 or HeLa cells dramatically decreases PARP activity in vivo, reinforcing the potential protective function of PARP at DNA breaks. Given that XRCC1 is also associated with DNA ligase III via a second BRCT module and with DNA polymerase beta , our results provide strong evidence that PARP is a member of a BER multiprotein complex involved in the detection of DNA interruptions and possibly in the recruitment of XRCC1 and its partners for efficient processing of these breaks in a coordinated manner. The modular organizations of these interactors, associated with small conserved domains, may contribute to increasing the efficiency of the overall pathway.

* Corresponding author. Mailing address: Ecole Supérieure de Biotechnologie de Strasbourg, UPR 9003 du Centre National de la Recherche Scientifique, Boulevard S. Brant, F-67400 Illkirch-Graffenstaden, France. Phone: (33) 388 655 368. Fax: (33) 388 655 343. E-mail: demurcia{at}esbs.u-strasbg.fr.

Mol Cell Biol, June 1998, p. 3563-3571, Vol. 18, No. 6
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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