Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis.
Rpn10, a subunit of the 26S proteasome, has been proposed to act as a receptor for multiubiquitin chains in ubiquitin-dependent proteolysis. However, studies on RPN10- deleted mutants in yeasts have suggested the presence of other multiubiquitin chain- binding factors functioning in ubiquitin-dependent proteolysis. Here, we report that a mutant with a triple deletion of RAD23, DSK2, and RPN10 genes accumulates large amounts of polyubiquitinated proteins, as is the case with a mutant with RAD23 and DSK2 deletions under restrictive conditions. Dsk2, Rad23, and Rpn10 have different capacities to bind multiubiquitin chains. Another ubiquitin-like protein, Ddi1, has similar activity to those of Rad23 and Dsk2. Taken together, the results suggest that ubiquitin-like proteins, Rad23, Dsk2, possibly Ddi1, and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis, serving as multiubiquitin chain-binding proteins.[1]References
- Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis. Saeki, Y., Saitoh, A., Toh-e, A., Yokosawa, H. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
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