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Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome

By Minoru Funakoshi, Toru Sasaki, Takeharu Nishimoto and Hideki Kobayashi


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

Topics: Biological Sciences
Publisher: The National Academy of Sciences
Year: 2002
DOI identifier: 10.1073/pnas.012585199
OAI identifier: oai:pubmedcentral.nih.gov:117376
Provided by: PubMed Central
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