The chromatin remodeler p400 ATPase facilitates Rad51-mediated repair of DNA double-strand breaks

Author:

Courilleau Céline11,Chailleux Catherine11,Jauneau Alain2,Grimal Fanny3,Briois Sébastien11,Boutet-Robinet Elisa44,Boudsocq François5,Trouche Didier11,Canitrot Yvan11

Affiliation:

1. Laboratoire de Biologie Cellulaire et Moléculaire du Contrôle de la Prolifération, UMR 5088, Université de Toulouse and Centre National de la Recherche Scientifique, Université Paul Sabatier, 31062 Toulouse, France

2. FR3450 Plateforme Microscopie imagerie, Pôle Biotechnologie Végétale, Centre National de la Recherche Scientifique, 31326 Castanet Tolosan, France

3. Centre de Recherche en Cancérologie de Toulouse, UMR 1037, Institut National de la Santé et de la Recherche Médicale, Université de Toulouse, 31024 Toulouse, France

4. Toxalim, Research Centre in Food Toxicology, UMR 1131, Institut National de la Recherche Agronomique and Université de Toulouse, 31027 Toulouse, France

5. Laboratoire de Biologie Moléculaire Eucaryote, UMR 5099, Centre National de la Recherche Scientifique, Université de Toulouse, 31062 Toulouse, France

Abstract

DNA damage signaling and repair take place in a chromatin context. Consequently, chromatin-modifying enzymes, including adenosine triphosphate–dependent chromatin remodeling enzymes, play an important role in the management of DNA double-strand breaks (DSBs). Here, we show that the p400 ATPase is required for DNA repair by homologous recombination (HR). Indeed, although p400 is not required for DNA damage signaling, DNA DSB repair is defective in the absence of p400. We demonstrate that p400 is important for HR-dependent processes, such as recruitment of Rad51 to DSB (a key component of HR), homology-directed repair, and survival after DNA damage. Strikingly, p400 and Rad51 are present in the same complex and both favor chromatin remodeling around DSBs. Altogether, our data provide a direct molecular link between Rad51 and a chromatin remodeling enzyme involved in chromatin decompaction around DNA DSBs.

Publisher

Rockefeller University Press

Subject

Cell Biology

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