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. 2013 Nov 1;24(21):3350–3357. doi: 10.1091/mbc.E13-05-0257

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© 2013 Ivanova et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 1: — Cdc10 is targeted by the DNA damage response. (A) Total RNA was prepared from untreated (–) or HU-treated (+) cultures of wild-type (WT) and Yox1.SATA (SATA) cells and analyzed by hybridization to the probes indicated on the left. rRNA is shown as loading control. (B) Loading of Cdc10 on cdc22 and cdc18 promoters was measured by chromatin immunoprecipitation analysis of chromatin extracts isolated from untreated or HU-treated (10 mM HU, 4 h at 30°C) cultures of WT, SATA, ∆cds1, ∆chk1, ∆cds1∆chk1, or ∆rad3 cells. Endogenous Cdc10 is HA tagged, and the levels of binding are quantified on anti-HA immunoprecipitated DNA. (C) The same chromatin extracts analyzed for Yox1 binding with anti-Yox1 polyclonal antibodies. (D) Phosphorylation level of endogenous Chk1-HA in native extracts prepared from untreated (−) or HU-treated (+) cultures of WT, SATA, or ∆cds1 strains. Proteins were resolved in 8% SDS–PAGE and anti-HA Western blotted to detect Chk1.