Abstract
Phosphorylation of H2AX functions to recruit DNA repair complexes to sites of DNA damage. Here, we report that H2AX is constitutively acetylated on lysine 36 (H2AXK36Ac) by the CBP/p300 acetyltransferases. H2AXK36Ac is required for cells to survive exposure to ionizing radiation; however, H2AXK36Ac levels are not increased by DNA damage. Further, acetylation of H2AX did not affect phosphorylation of H2AX or the formation of DNA damage foci. Finally, cells with a double mutation in both the H2AX acetylation and phosphorylation sites were more radiosensitive than cells containing individual mutations. H2AXK36Ac is therefore a novel, constitutive histone modification located within the histone core region which regulates radiation sensitivity independently of H2AX phosphorylation.
Original language | English (US) |
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Pages (from-to) | 2926-2930 |
Number of pages | 5 |
Journal | FEBS letters |
Volume | 584 |
Issue number | 13 |
DOIs | |
State | Published - Jul 2010 |
Externally published | Yes |
Keywords
- Acetylation
- Chromatin
- DNA double-strand break
- H2AX
- Histone acetyltransferase
- IR
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology