title: Acetylation of H2AX on lysine 36 plays a key role in the DNA double-strand break repair pathway.
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.
authors.affiliation: Division of Genomic Stability and DNA Repair, Department of Radiation Oncology, Dana-Farber Cancer Institute, Boston, MA 02115, USA.
authors.forename: Xiaofeng
authors.initials: X
authors.lastname: Jiang
authors.forename: Ye
authors.initials: Y
authors.lastname: Xu
authors.forename: Brendan D
authors.initials: BD
authors.lastname: Price
mesh_terms: D000107:Acetylation; D015153:Blotting, Western; D002460:Cell Line; D053903:DNA Breaks, Double-Stranded; D004260:DNA Repair / Q000235:genetics / Q000502:physiology*; D006657:Histones / Q000378:metabolism*; D006801:Humans; D015398:Signal Transduction / Q000235:genetics / Q000502:physiology*
chemical_list: C468783:H2AX protein, human; D006657:Histones