Abstract
Dsk2p from Saccharomyces cerevisiae belongs to the class of proteins that contain a ubiquitin-like (UbL) domain at the N terminus together with a ubiquitin-associated (UBA) domain at the C terminus. We show here that the C-terminal UBA domain of Dsk2p binds to K48-linked polyubiquitin chains, and the N-terminal UbL domain of Dsk2p interacts with the proteasome. Overexpression of Dsk2p caused the accumulation of large amounts of polyubiquitin, and extragenic suppressors of the Dsk2p-mediated lethality proved to be temperature-sensitive mutations in two proteasome subunits, rpn1 and pre2. K48-linked ubiquitin-dependent degradation was impaired by disruption of the DSK2 gene. These results indicate that Dsk2p is K48-linked polyubiquitin-binding protein and also interacts with the proteasome. We discuss a possible role of adaptor function of Dsk2p via its UbL and UBA domains in the ubiquitin-proteasome pathway.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 26, 2002, 10:36 a.m.) |
Deposited | 3 years, 4 months ago (April 12, 2022, 9:02 a.m.) |
Indexed | 3 months, 1 week ago (May 16, 2025, 2:41 p.m.) |
Issued | 23 years, 7 months ago (Jan. 22, 2002) |
Published | 23 years, 7 months ago (Jan. 22, 2002) |
Published Online | 23 years, 7 months ago (Jan. 22, 2002) |
Published Print | 23 years, 7 months ago (Jan. 22, 2002) |
@article{Funakoshi_2002, title={Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome}, volume={99}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.012585199}, DOI={10.1073/pnas.012585199}, number={2}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Funakoshi, Minoru and Sasaki, Toru and Nishimoto, Takeharu and Kobayashi, Hideki}, year={2002}, month=jan, pages={745–750} }