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

Abstract：

: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.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Downs JA,Allard S,Jobin-Robitaille O,Javaheri A,Auger A,Bouchard N,Kron SJ,Jackson SP,Côté J

doi

10.1016/j.molcel.2004.12.003

subject

Has Abstract

pub_date

2004-12-22 00:00:00

pages

979-90

issue

6

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(04)00758-0

journal_volume

16

pub_type

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