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M404524200v1
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Papers In Press, published online ahead of print October 21, 2004
J. Biol. Chem, 10.1074/jbc.M404524200
Submitted on April 23, 2004
Revised on October 19, 2004
Accepted on October 20, 2004

Involvement of PARP-1 and XRCC1/DNA ligase III in an alternative route for DNA double-strand breaks rejoining

Marc Audebert, Bernard Salles, and Patrick Calsou

IPBS, CNRS UMR 5089, Toulouse 31077

Corresponding Author: bernard.salles{at}ipbs.fr

The efficient repair of DNA double-strand breaks (DSBs) is critical for the maintenance of genomic integrity. In mammalian cells, the non-homologous end-joining (NHEJ) process that represents the predominant repair pathway relies on the DNA-dependent protein kinase (DNA-PK) and the XRCC4/DNA ligase IV complex. Nonetheless, several in vitro and in vivo results indicate that mammalian cells use more than a single end-joining mechanism. While searching for a DNA-PK-independent end-joining activity, we found that the pre-treatment of DNA-PK proficient and deficient rodent cells with an inhibitor of the poly(ADP-ribose) polymerase-1 enzyme (PARP-1) led to increased cytotoxicity of the highly efficient DNA double-strand breaking compound calicheamicin g1. In addition, the repair kinetics of the DSBs induced by calicheamicin g1 was delayed both in PARP-1 proficient cells pretreated with the PARP-1 inhibitor and in PARP-1 deficient cells. In order to get new insights into the mechanism of an alternative route for DSBs repair, we have established a new synapsis and end-joining two-step assay in vitro, operating on DSBs with either nuclear protein extracts or recombinant proteins. We found an end-joining activity independent of the DNA-PK/XRCC4/Ligase IV complex but that actually required a novel synapsis activity of PARP-1 and the ligation activity of the XRCC1/DNA ligase III complex, proteins otherwise involved in the base excision repair pathway. Taken together, these results strongly suggest that a PARP-1-dependent DSBs end-joining activity may exist in mammalian cells. We propose that this mechanism could act as an alternative route of DSBs repair that complements the DNA-PK/XRCC4/Ligase IV dependent NHEJ.


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