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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
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 *
Florence
Le Page §,
Valérie
Schreiber¶,
Claudine
Dhérin ,
Gilbert
de Murcia¶, and
Serge
Boiteux
From the 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  / (Pol / ),
poly(ADP-ribose) polymerase-1 /
(PARP-1 / ), and
Pol / 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 Pol or PARP-1
or both. Whereas 8-oxoG repair in NTS is normal in Pol -null cells,
it is delayed in PARP-1-null cells and greatly impaired in cells
deficient in both Pol 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 / Pol / cell
lines. However, 8-oxoG repair is incomplete, yielding plasmid molecules
with a nick at the site of the lesion. Therefore,
PARP-1 / Pol / 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 Pol / 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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Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
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