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Biochem Biophys Res Commun. 2009 Mar 20;380(4):752-7. doi: 10.1016/j.bbrc.2009.01.109. Epub 2009 Jan 23.

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

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1
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
DOI:
10.1016/j.bbrc.2009.01.109
[Indexed for MEDLINE]
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