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. 2016 May 15;30(10):1211–1224. doi: 10.1101/gad.280685.116

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© 2016 Tsabar et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 5. — Coimmunoprecipitation of Asf1-HA and Rad53. Samples were run on 10% SDS-PAGE gels. Immunoprecipitation performed with anti-HA-conjugated agarose beads and blotted with anti-HA (Asf1-HA) or anti-Rad53. (A) Coimmunoprecipitation of Asf1-HA and Rad53 in an irreparable DSB system (JKM179). (B) Coimmunoprecipitation of Asf1-HA and Rad53 in a system with one repairable ectopic GC DSB (YJK17) and two repairable DSBs (YFA01). (C) Coimmunoprecipitation of Asf1-HA and Rad53 in a system with two repairable DSBs in rtt101Δ (left panel) or rtt109Δ (right panel). (D) Quantification of Rad53 association with Asf1. Rad53 immunoprecipitation signal was normalized to Asf1 immunoprecipitation signal and 0 h. Error bars indicate ranges. n = 2. (E) Fold increase of Rad53 levels. Rad53 levels were normalized to 0 h. Protein loading was quantified using a Bradford assay. Error bars indicate ranges. n = 2.