Journal
MOLECULAR CELL
Volume 16, Issue 6, Pages 1017-1025Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2004.12.007
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Funding
- NCI NIH HHS [CA95175, CA92625, P01 CA092625, R01 CA095175, R01 CA095175-03, P01 CA109901, CA109901] Funding Source: Medline
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Histone H2AX has a role in suppressing genomic instability and cancer. However, the mechanisms by which it performs these functions are poorly understood. After DNA breakage, H2AX is phosphorylated on serine 139 in chromatin near the break. We show here that H2AX serine 139 enforces efficient homologous recombinational repair of a chromosomal double-strand break (DSB) by using the sister chromatid as a template. BRCA1, Rad51, and CHK2 contribute to recombinational repair, in part independently of H2AX H2AX(-/-) cells show increased use of single-strand annealing, an error-prone deletional mechanism of DSB repair. Therefore, the chromatin response around a chromosomal DSB, in which H2AX serine 139 phosphorylation plays a central role, shapes the repair process in favor of potentially error-free interchromatid homologous recombination at the expense of error-prone repair. H2AX phosphorylation may help set up a favorable disposition between sister chromatids.
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