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Originally published In Press as doi:10.1074/jbc.M212905200 on March 7, 2003

J. Biol. Chem., Vol. 278, Issue 20, 18471-18477, May 16, 2003
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Poly(ADP-ribose) Polymerase-1 (PARP-1) Is Required in Murine Cell Lines for Base Excision Repair of Oxidative DNA Damage in the Absence of DNA Polymerase beta *

Florence Le PageDagger §, Valérie Schreiber, Claudine DhérinDagger , Gilbert de Murcia, and Serge BoiteuxDagger

From the Dagger  Commissariat à l'Energie Atomique (CEA), Direction des Sciences du Vivant, Département de Radiobiologie et Radiopathologie, Unité Mixte de Recherche 217 CNRS-CEA Radiobiologie Moléculaire et Cellulaire, 92265 Fontenay aux Roses, France and  Unité Propre de Recherche 9003, CNRS, Université Louis Pasteur, Ecole Supérieur de Biotechnologie de Strasbourg, 67400 Illkirch, France

Oxidative DNA base damage is mainly corrected by the base excision repair (BER) pathway, which can be divided into two subpathways depending on the length of the resynthetized patch, either one nucleotide for short patch BER or several nucleotides for long patch BER. The role of proteins in the course of BER processes has been investigated in vitro using purified enzymes and cell-free extracts. In this study, we have investigated the repair of 8-oxo-7,8-dihydroguanine (8-oxoG) in vivo using wild-type, polymerase beta -/- (Polbeta -/-), poly(ADP-ribose) polymerase-1-/- (PARP-1-/-), and Polbeta -/-PARP-1-/- 3T3 cell lines. We used non replicating plasmids containing a 8-oxoG:C base pair to study the repair of the lesion located in a transcribed sequence (TS) or in a non-transcribed sequence (NTS). The results show that 8-oxoG repair in TS is not significantly impaired in cells deficient in Polbeta or PARP-1 or both. Whereas 8-oxoG repair in NTS is normal in Polbeta -null cells, it is delayed in PARP-1-null cells and greatly impaired in cells deficient in both Polbeta and PARP-1. The removal of 8-oxoG and presumably the cleavage at the resulting apurinic/apyrimidinic site are not affected in the PARP-1-/-Polbeta -/- cell lines. However, 8-oxoG repair is incomplete, yielding plasmid molecules with a nick at the site of the lesion. Therefore, PARP-1-/-Polbeta -/- cell lines cannot perform 5'-dRP removal and/or DNA repair synthesis. Furthermore, the poly(ADP-ribosyl)ation activity of PARP-1 is essential for 8-oxoG repair in a Polbeta -/- context, because expression of the catalytically inactive PARP-1 (E988K) mutant does not restore 8-oxoG repair, whereas an wild type PARP-1 does.

* This work was supported by CNRS and CEA, the Association pour la Recherche sur le Cancer (ARC) Grant 5432 (to S. B.) and European Commission Grant FIGH-CT-2002-00207, and additional funds from CNRS, the Association pour la Recherche Contre le Cancer, Electricité de France, Ligue Nationale Contre le Cancer, and Commissariat à l'Energie Atomique (to G. d. M.).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: 00331-46548939; Fax: 00331-46548859; E-mail: lepage@dsvidf.cea.fr.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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