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WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activity

Andrew Xiao, Haitao Li, David Shechter, Sung Hee Ahn, Laura A. Fabrizio, Hediye Erdjument-Bromage, Satoko Ishibe-Murakami, Bin Wang, Paul Tempst, Kay Hofmann, Dinshaw J. Patel, Stephen J. Elledge & C. David Allis

Nature 457, 57-62(1 January 2009)

doi:10.1038/nature07668

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Figure 1 - Unfortunately we are unable to provide accessible alternative text for this. If you require assistance to access this image, or to obtain a text description, please contact npg@nature.com

Figure 1

Tyr 142 of H2A.X is a new phosphorylation mark regulated by DNA damage signals.

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Figure 2

The WSTF–SNF2H chromatin remodelling complex is specifically associated with H2A.X nucleosomes in vivo.

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Figure 3

WSTF contains a kinase domain that phosphorylates Tyr 142 of H2A.X.

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Figure 4

WSTF is critical for the maintenance of bold gamma-H2A.X phosphorylation after DNA damage.

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