Abstract
The repair of DNA double-strand breaks (DSBs) requires remodeling of the local chromatin architecture to allow the repair machinery to access sites of damage. Here, we report that the histone variant macroH2A1.1 is recruited to DSBs. Cells lacking macroH2A1 have defective recruitment of 53BP1, defective activation of chk2 kinase and increased radiosensitivity. Importantly, macroH2A1.1 is not incorporated into nucleosomes at DSBs, but instead associates with the chromatin through a mechanism which requires PARP1 activity. These results reveal an unusual mechanism involving a direct association of macroH2A1.1 with PARylated chromatin which is critical for retaining 53BP1 at sites of damage.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 3920-3925 |
| Number of pages | 6 |
| Journal | FEBS letters |
| Volume | 586 |
| Issue number | 21 |
| DOIs | |
| State | Published - Nov 2 2012 |
| Externally published | Yes |
Keywords
- 53BP1
- DNA repair
- Ionizing radiation
- MacroH2A1
- Nucleosome
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
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Cite this
Xu, C., Xu, Y., Gursoy-Yuzugullu, O., & Price, B. D. (2012). The histone variant macroH2A1.1 is recruited to DSBs through a mechanism involving PARP1. FEBS letters, 586(21), 3920-3925. https://doi.org/10.1016/j.febslet.2012.09.030