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    Biochem Biophys Res Commun. 2009 Mar 20;380(4):752-7. Epub 2009 Jan 23.

    Histone H2AX participates the DNA damage-induced ATM activation through interaction with NBS1.

    Kobayashi J, Tauchi H, Chen B, Burma S, Tashiro S, Matsuura S, Tanimoto K, Chen DJ, Komatsu K.

    Source

    Department of Genome Repair Dynamics, Radiation Biology Center, Kyoto University, Kyoto 606-8501, Japan. jkobayashi@house.rbc.kyoto-u.ac.jp

    Erratum in

    • Biochem Biophys Res Commun. 2009 Jun 26;384(2):271. Bruma, Sandeep [corrected to Burma, Sandeep].

    Abstract

    Phosphorylated histone H2AX (gamma-H2AX) functions in the recruitment of DNA damage response proteins to DNA double-strand breaks (DSBs) and facilitates DSB repair. ATM also co-localizes with gamma-H2AX at DSB sites following its auto-phosphorylation. However, it is unclear whether gamma-H2AX has a role in activation of ATM-dependent cell cycle checkpoints. Here, we show that ATM as well as NBS1 is recruited to damaged-chromatin in a gamma-H2AX-dependent manner. Foci formation of phosphorylated ATM and ATM-dependent phosphorylation is repressed in H2AX-knockdown cells. Furthermore, anti-gamma-H2AX antibody co-immunoprecipitates an ATM-like protein kinase activity in vitro and recombinant H2AX increases in vitro kinase activity of ATM from un-irradiated cells. Moreover, H2AX-deficient cells exhibited a defect in ATM-dependent cell cycle checkpoints. Taken together, gamma-H2AX has important role for effective DSB-dependent activation of ATM-related damage responses via NBS1.

    PMID:
    19338747
    [PubMed - indexed for MEDLINE]

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