文章基本信息

标题：Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
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作者：Minoru Funakoshi ; Toru Sasaki ; Takeharu Nishimoto 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2002
卷号：99
期号：2
页码：745-750
DOI：10.1073/pnas.012585199
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
关键词：ubiquitin-related protein‖polyubiquitin adaptor‖UBA domain‖ ubiquitin chains‖UbL domain