Supplementary information

From the following article:

A phosphatase complex that dephosphorylates gammaH2AX regulates DNA damage checkpoint recovery

Michael-Christopher Keogh, Jung-Ae Kim, Michael Downey, Jeffrey Fillingham, Dipanjan Chowdhury, Jacob C. Harrison, Megumi Onishi, Nira Datta, Sarah Galicia, Andrew Emili, Judy Lieberman, Xuetong Shen, Stephen Buratowski, James E. Haber, Daniel Durocher, Jack F. Greenblatt & Nevan J. Krogan

Nature 439, 497-501(26 January 2006)

doi:10.1038/nature04384

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Supplementary Notes

Additional details on the methods used in this study and Supplementary Figure Legends.

Supplementary Table 1

Yeast strains.

Supplementary Figure 1

Specificity of Pph3 for gammaH2AX and optimization of Pph3 reaction conditions.

Supplementary Figure 2

The HTP-C interacts with DNA repair and replication factors.

Supplementary Figure 3

The HTP-C associates with its histone H2A substrate

Supplementary Figure 4

The HTP-C associates with its histone H2A substrate.

Supplementary Figure 5

gammaH2AX is lost from the chromatin surrounding a DSB in rad54delta cells, even though this mutant is unable to complete DSB repair.

Supplementary Figure 6

The lower levels of gammaH2AX immediately adjacent to a DSB are independent of Pph3.

Supplementary Figure 7

Pph3 is not required for checkpoint adaptation.

Supplementary Figure 8

Pph3 specificity for gammaH2AX.

Supplementary Figure 9

The majority of gammaH2AX in cells is chromatin-associated.

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