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. 2008 Sep 8;182(5):873–883. doi: 10.1083/jcb.200801054

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© 2008 Queralt and Uhlmann

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 7. — Interactions between separase, Zds1, and Cdc55. (A) Zds1 and Cdc55 interact independently of separase. Co-immunoprecipitation between Zds1 and Cdc55 was analyzed in protein extracts from strains Y585 (MATa Zds1-Pk₆ HA₃-CDC55) and Y586 (as 585, but esp1-2) that were grown at 33°C, a restrictive temperature for the separase esp1-2 allele, for 1 h before extract preparation. Protein extracts from strain Y584 (MATa HA₃-CDC55) lacking a Pk epitope on Zds1 served as a control. (B) Separase and Cdc55 interact independently of Zds1 and Zds2. (B) As (A), but Cdc55 co-immuoprecipitation with separase from extracts of strains Y587 (MATa ESP1-HA₆), Y3434 (as 587, but Pk₃-CDC55), and Y3427 (as 3434, but zds1Δ zds2Δ) grown at 25°C was analyzed. (C) An interaction between separase and Zds1. Co-immunoprecipitation of separase with Zds1 was analyzed in extracts from strains Y587 (MATa ESP1-HA₆), Y588 (as 587, but Zds1-Pk₆), and Y589 (as 588, but cdc55Δ).