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. 2018 Oct 12;400(4):487–500. doi: 10.1515/hsz-2018-0251

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©2019 Annemarie Wolmarans et al., published by De Gruyter, Berlin/Boston

This work is licensed under the Creative Commons Attribution 4.0 International License.

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Figure 6: — The cooperative displacement of Sti1p from SUMOylated Hsp82p and a model for SUMO regulation of the ATPase cycle.

(A) Effective displacement of Sti1p by Cpr6p and Aha1p restore ATPase activity of SUMOylated Hsp82p^K178C to a similar degree as non-SUMOylated Hsp82p^K178C. Reactions contained 1 μm Hsp82p^K178C (black) or Hsp82p^K178C-Smt3p^Cys (gray) and 4 μm Sti1p, Cpr6p, and Aha1p where indicated. Each scatter plot shows the average and standard deviation from three triplicate experiments (n=3). (B) A model of the role SUMOylation has on its ATPase cycle of Hsp90. SUMOylation of yeast Hsp90 at K178 does not interfere with Sti1p displacement, but results in a stable recruitment of Aha1p which hinders Sba1p inhibition.