Acetylation of H2AX on lysine 36 plays a key role in the DNA double-strand break repair pathway

Xiaofeng Jiang, Ye Xu, Brendan D. Price

Research output: Contribution to journalArticlepeer-review

27 Scopus citations


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 languageEnglish (US)
Pages (from-to)2926-2930
Number of pages5
JournalFEBS letters
Issue number13
StatePublished - Jul 2010
Externally publishedYes


  • Acetylation
  • Chromatin
  • DNA double-strand break
  • H2AX
  • Histone acetyltransferase
  • IR

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


Dive into the research topics of 'Acetylation of H2AX on lysine 36 plays a key role in the DNA double-strand break repair pathway'. Together they form a unique fingerprint.

Cite this