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. 2015 Jul 15;26(14):2609–2619. doi: 10.1091/mbc.E14-07-1213

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© 2015 Al-Zain 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 4: — DNA damage triggers Cdc6 degradation in Mck1-dependent manner. (A) CDC6-prA or Δmck1 CDC6-prA cells were incubated in yeast extract/peptone/dextrose (YEPD) medium to log phase, and then MMS was added (0.05% final). Protein extracts were made at 0-, 30-, or 60-min incubation and subjected to Western blotting to visualize endogenous Cdc6-prA. Pgk1 was used as a loading control. The same experiment was repeated three times to quantify Cdc6 protein levels. Average percentage of Cdc6p remaining is shown. Bars represent SD. (B) Protein degradation of Orc6-prA or Mck1-9MYC was examined by the same method using IgG or anti-MYC antibodies, respectively. (C) CDC6-prA or CDC6-T368A-prA cells were grown in YEPD to log phase. MMS at 0.1% concentration was added, and protein samples were collected after 0, 30, and 60 min. The protein extracts were subjected to Western blotting to visualize Cdc6-prA. The same experiment was performed three times. Cdc6 protein levels were quantified, and average percentage of Cdc6p remaining is shown. Bars represent SD.