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Originally published In Press as doi:10.1074/jbc.M202390200 on April 10, 2002

J. Biol. Chem., Vol. 277, Issue 25, 23028-23036, June 21, 2002
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Poly(ADP-ribose) Polymerase-2 (PARP-2) Is Required for Efficient Base Excision DNA Repair in Association with PARP-1 and XRCC1*

Valérie SchreiberDagger , Jean-Christophe AméDagger , Pascal Dollé§, Inès SchultzDagger , Bruno RinaldiDagger , Valérie Fraulob§, Josiane Ménissier-de MurciaDagger , and Gilbert de MurciaDagger

From the Dagger  UPR 9003 du Centre National de la Recherche Scientifique, Laboratoire conventionné avec le Commissariat à l'Energie Atomique, Université Louis Pasteur, Ecole Supérieure de Biotechnologie de Strasbourg, boulevard Sébastien Brant, F-67400 Illkirch and the § Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, Collège de France, BP 163, 67404 Illkirch cedex, France

The DNA damage dependence of poly(ADP-ribose) polymerase-2 (PARP-2) activity is suggestive of its implication in genome surveillance and protection. Here we show that the PARP-2 gene, mainly expressed in actively dividing tissues follows, but to a smaller extent, that of PARP-1 during mouse development. We found that PARP-2 and PARP-1 homo- and heterodimerize; the interacting interfaces, sites of reciprocal modification, have been mapped. PARP-2 was also found to interact with three other proteins involved in the base excision repair pathway: x-ray cross complementing factor 1 (XRCC1), DNA polymerase beta , and DNA ligase III, already known as partners of PARP-1. XRCC1 negatively regulates PARP-2 activity, as it does for PARP-1, while being a polymer acceptor for both PARP-1 and PARP-2. To gain insight into the physiological role of PARP-2 in response to genotoxic stress, we developed by gene disruption mice deficient in PARP-2. Following treatment by the alkylating agent N-nitroso-N-methylurea (MNU), PARP-2-deficient cells displayed an important delay in DNA strand breaks resealing, similar to that observed in PARP-1 deficient cells, thus confirming that PARP-2 is also an active player in base excision repair despite its low capacity to synthesize ADP-ribose polymers.

* This work was supported by Association pour la Recherche Contre le Cancer, Ligue Nationale contre le Cancer et Comité Régional, Electricité de France, Commissariat à l'Energie Atomique and Centre National de la Recherche Scientifique.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.

To whom correspondence should be addressed. Tel.: 33-390-24-47-07; Fax: 33-390-24-46-86; E-mail: demurcia@esbs.u-strasbg.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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