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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Sasaki, Toru Nishimoto, Takeharu Funakoshi, Minoru Kobayashi, Hideki |
| Description | Author Affiliation: Funakoshi M ( Department of Molecular Biology, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan.); |
| 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. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 2 |
| Volume Number | 99 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2002-01-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cell Cycle Proteins Cysteine Endopeptidases Metabolism Fungal Proteins Multienzyme Complexes Saccharomyces Cerevisiae Proteins Ubiquitins Binding Sites Chemistry Genetics DNA-Binding Proteins Genes, Fungal Genes, Suppressor Mutation Proteasome Endopeptidase Complex Protein Structure, Tertiary Protein Subunits Proteins Recombinant Proteins Temperature Two-Hybrid System Techniques Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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