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. 2015 May 15;43(12):5759–5770. doi: 10.1093/nar/gkv498

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© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 8. — Effect of HMO1 C-terminal tail on H2A phosphorylation and Rad51 recruitment. (A) ChIP with DDY3 WT and AB strain expressing HMO1 deleted for its C-terminal tail using antibody to phosphorylated H2A at MAT and 29.5 kb upstream of DSB during DNA damage (galactose) and repair (glucose). IC, input control; No, no antibody; IP, immunoprecipitation with antibody to γ-H2AX. (B) Densitometric analysis of ChIP data shown in (A), obtained with ImageJ software. (C) ChIP with DDY3 WT and AB strain using antibody to Rad51 at MAT during DNA damage (galactose). (D) Densitometric analysis of ChIP data shown in (C). Fold enrichment = ChIP/Input DNA. Three independent experiments were performed. Error bars represent standard deviation.