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. 2018 Sep 7;7:e35447. doi: 10.7554/eLife.35447

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© 2018, Wang et al

This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.

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Figure 8. — A stable interaction between chromatin and the SAP domain of Siz1 stimulates its activity to modify Rpc53 with SUMO (S). Rpc53 sumoylation triggers ubiquitin (U) modification of Rpc160 and potentially other proteins by the Slx5-Slx8 complex, which also required the interaction between chromatin and the DNA-binding domain (DBD) of Slx8. Ubiquitylation subsequently activates Cdc48 to disassemble the Pol III complex, facilitating degradation of Pol III subunits by the proteasome.