Histone H2A.Z controls a critical chromatin remodeling step required for DNA double-strand break repair.
Histone H2A.Z controls a critical chromatin remodeling step required for DNA double-strand break repair.
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DOI:
10.1016/j.molcel.2012.09.026
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发表时间:
2012-12-14
期刊:
影响因子:
16
通讯作者:
Price, Brendan D.
中科院分区:
文献类型:
--
作者:
Xu, Ye;Ayrapetov, Marina K.;Xu, Chang;Gursoy-Yuzugullu, Ozge;Hu, Yiduo;Price, Brendan D.
Chromatin remodeling during DNA double-strand break (DSB) repair is required to facilitate access to and repair of DSBs. This remodeling requires increased acetylation of histones and a shift in nucleosome organization to create open, relaxed chromatin domains. However, the underlying mechanism driving changes in nucleosome structure at DSBs is poorly defined. Here, we demonstrate that histone H2A.Z is exchanged onto nucleosomes at DSBs by the p400 remodeling ATPase. H2A.Z exchange at DSBs shifts the chromatin to an open conformation, and is required for acetylation and ubiquitination of histones and for loading of the brca1 complex. H2A.Z exchange also restricts single-stranded DNA production by nucleases and is required for loading of the Ku70/80 DSB repair protein. H2A.Z exchange therefore promotes specific patterns of histone modification and reorganization of the chromatin architecture, leading to the assembly of a chromatin template which is an efficient substrate for the DSB repair machinery.
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影响因子:
16
作者:
Downs, JA;Allard, S;Côté, J
通讯作者:
Côté, J
影响因子:
7
作者:
Lee, Hyung Joo;Kim, Eunji;Kim, Jin-Soo
通讯作者:
Kim, Jin-Soo
影响因子:
16.8
作者:
通讯作者:
--
DOI:
10.1007/978-1-60327-015-1_19
发表时间:
2009-01-01
期刊:
DNA-PROTEIN INTERACTIONS: PRINCIPLES AND PROTOCOLS, THIRD EDITION
影响因子:
--
作者:
Gevry, Nicolas;Svotelis, Amy;Gaudreau, Luc
通讯作者:
Gaudreau, Luc
影响因子:
10.5
作者:
Keogh, MC;Mennella, TA;Buratowski, S
通讯作者:
Buratowski, S