Binding of chromatin-modifying activities to phosphorylated histone H2A at DNA damage sites

Jessica A. Downs, Stéphane Allard, Olivier Jobin-Robitaille, Ali Javaheri, Andréanne Auger, Nathalie Bouchard, Stephen J. Kron, Stephen P. Jackson, Jacques Côté

Research output: Contribution to journalArticlepeer-review

460 Scopus citations


Yeast histone H2A is phosphorylated on Ser129 upon DNA damage, an event required for efficient repair. We show that phosphorylation occurs rapidly over a large region around DNA double-strand breaks (DSBs). Histone H4 acetylation is also important for DSB repair, and we found that the NuA4 HAT complex associates specifically with phospho-H2A peptides. A single NuA4 subunit, Arp4, is responsible for the interaction. The NuA4 complex is recruited to a DSB concomitantly with the appearance of H2A P-Ser129 and Arp4 is important for this binding. Arp4 is also a subunit of the Ino80 and Swr1 chromatin remodeling complexes, which also interact with H2A P-Ser129 and are recruited to DSBs. This association again requires Arp4 but also prior NuA4 recruitment and action. Thus, phosphorylation of H2A at DNA damage sites creates a mark recognized by different chromatin modifiers. This interaction leads to stepwise chromatin reconfiguration, allowing efficient DNA repair.

Original languageEnglish
Pages (from-to)979-990
Number of pages12
JournalMolecular cell
Issue number6
StatePublished - Dec 22 2004


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