The histone variant macroH2A1.1 is recruited to DSBs through a mechanism involving PARP1

Chang Xu, Ye Xu, Ozge Gursoy-Yuzugullu, Brendan D. Price

Research output: Contribution to journalArticle

37 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)3920-3925
Number of pages6
JournalFEBS Letters
Volume586
Issue number21
DOIs
StatePublished - Nov 2 2012
Externally publishedYes

Fingerprint

Histones
Chromatin
Chromatin Assembly and Disassembly
Double-Stranded DNA Breaks
Nucleosomes
Radiation Tolerance
Repair
Phosphotransferases
Machinery
Chemical activation
Association reactions
DNA

Keywords

  • 53BP1
  • DNA repair
  • Ionizing radiation
  • MacroH2A1
  • Nucleosome

ASJC Scopus subject areas

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

Cite this

The histone variant macroH2A1.1 is recruited to DSBs through a mechanism involving PARP1. / Xu, Chang; Xu, Ye; Gursoy-Yuzugullu, Ozge; Price, Brendan D.

In: FEBS Letters, Vol. 586, No. 21, 02.11.2012, p. 3920-3925.

Research output: Contribution to journalArticle

Xu, Chang ; Xu, Ye ; Gursoy-Yuzugullu, Ozge ; Price, Brendan D. / The histone variant macroH2A1.1 is recruited to DSBs through a mechanism involving PARP1. In: FEBS Letters. 2012 ; Vol. 586, No. 21. pp. 3920-3925.
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