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

被引：56
|
作者：
Xu, Chang [1 ,2 ,3 ]
Xu, Ye [1 ]
Gursoy-Yuzugullu, Ozge [1 ]
Price, Brendan D. [1 ]
机构：
[1] Harvard Univ, Sch Med, Dana Farber Canc Inst, Dept Radiat Oncol, Boston, MA 02215 USA
[2] Chinese Acad Med Sci, Inst Radiat Med, Tianjin 300192, Peoples R China
[3] Peking Union Med Coll, Tianjin Key Lab Mol Nucl Med, Tianjin 300192, Peoples R China
来源：
FEBS LETTERS | 2012年 / 586卷 / 21期
关键词：
DNA repair; MacroH2A1; Ionizing radiation; 53BP1; Nucleosome; DOUBLE-STRAND BREAKS; DNA-DAMAGE; CHROMATIN; 53BP1; ACTIVATION; REPAIR; PROTEINS; MAINTENANCE; METHYLATION; CHECKPOINT;
D O I：
10.1016/j.febslet.2012.09.030
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
收藏
页码：3920 / 3925
页数：6
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