Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome
| Autor: | Kylie J. Walters, Bradley B. Stocks, Shuangwu Sun, John R. Engen, Yuan Shi, Byung-Hoon Lee, Sergey G. Tarasov, Jacob Vannoy, Daniel Finley, Fabian Tuebing, Suzanne Elsasser, Yanhong Shi, Xiang Chen, Naixia Zhang, Stefanie A. H. de Poot, Geng Tian |
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| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular 0301 basic medicine Proteasome Endopeptidase Complex Ubiquitin-Specific Proteases Saccharomyces cerevisiae Proteins Saccharomyces cerevisiae Ubiquitin-conjugating enzyme Article Deubiquitinating enzyme 03 medical and health sciences Ubiquitin Endopeptidases Multidisciplinary 030102 biochemistry & molecular biology biology Ubiquitination Cell biology Ubiquitin ligase DNA-Binding Proteins Ubiquitins 030104 developmental biology Proteasome Biochemistry Mutation biology.protein Metabolic Networks and Pathways Deubiquitination |
| Zdroj: | Science. 351 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.aad9421 |
| Popis: | The yin and yang of proteasomal regulation The ubiquitin-proteasome pathway regulates myriad proteins through their selective proteolysis. The small protein ubiquitin is attached, typically in many copies, to the target protein, which is then recognized and broken down by the proteasome. Shi et al. found a repeat structure in the proteasome for recognizing ubiquitin as well as ubiquitin-like (UBL) proteins. Tandem binding sites allow the proteasome to dock multiple proteins. One of the bound UBL proteins is an enzyme that cleaves ubiquitin-protein conjugates, which antagonizes degradation. Thus, the repetition of related binding sites with distinct specificity achieves a balance of positive and negative regulation of the proteasome. Science , this issue p. 10.1126/science.aad9421 |
| Databáze: | OpenAIRE |
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