Budding Yeast Dsk2p is a Polyubiquitin-binding Protein That Can Interact with the Proteasome

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2002 Jan 24

PMID 11805328

Citations 112

Authors

Minoru Funakoshi

Toru Sasaki

Takeharu Nishimoto

Hideki Kobayashi

Affiliations

Soon will be listed here.

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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