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The γ‐H2A.X: Is it just a surrogate marker of double‐strand breaks or much more?
Author(s) -
Ismail Ismail Hassan,
Hendzel Michael J
Publication year - 2008
Publication title -
environmental and molecular mutagenesis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1
H-Index - 87
eISSN - 1098-2280
pISSN - 0893-6692
DOI - 10.1002/em.20358
Subject(s) - histone h2a , histone , histone code , phosphorylation , biology , histone h3 , microbiology and biotechnology , dna repair , histone methylation , histone h1 , histone methyltransferase , dna , genetics , nucleosome , gene , dna methylation , gene expression
Abstract In recent years, several histone modifications have been implicated in the cellular response to DNA double‐strand breaks (DSBs). One of the best characterized histone modifications important in DSB repair is the phosphorylation of histone H2A variant, H2A.X. In response to DSBs, H2A.X is phosphorylated and this phosphorylation is required for DSB signaling and the retention of repair proteins at the break site. Despite the existing picture that the function of H2A.X is to promote DNA repair, very recent data suggest that the phosphorylation of histone H2A.X has additional functions. This is analogous to histone H3 phosphorylation on serine 10, which participates in seemingly incompatible functions—transcriptional activation and mitosis. In this review, we discuss the role of histone H2A.X in maintaining genomic stability and review emerging evidence that histone H2A.X is multifunctional. Environ. Mol. Mutagen., 2008. © 2007 Wiley‐Liss, Inc.