Journal
FEBS LETTERS
Volume 584, Issue 13, Pages 2926-2930Publisher
WILEY
DOI: 10.1016/j.febslet.2010.05.017
Keywords
H2AX; Acetylation; Chromatin; DNA double-strand break; Histone acetyltransferase; IR
Funding
- NCI [CA64585, CA93602]
- DOD
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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. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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