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Binding of chromatin-modifying activities to phosphorylated histone H2A at DNA damage sites
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posted on 2023-06-08, 09:17 authored by Jessica A Downs, Stéphane Allard, Olivier Jobin-Robitaille, Ali Javaheri, Andréanne Auger, Nathalie Bouchard, Stephen J Kron, Stephen P Jackson, Jacques CôtéYeast 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.
History
Publication status
- Published
Journal
Molecular CellISSN
1097-2765External DOI
Issue
6Volume
16Page range
979-990Pages
12.0Department affiliated with
- Sussex Centre for Genome Damage Stability Publications
Notes
The work was initiated by JD, whoorganized the collaboration with the Cote lab. The design and interpretation of experiments and the manuscript preparation were done almost entirely by me and Prof. Cote. The data in approximately half of the figures in the manuscript were generated by JD.Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2012-02-06Usage metrics
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