Article
Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome.
Science (New York, N.Y.) - 19 Feb 2016
Shi Yuan, Chen Xiang, Elsasser Suzanne, Stocks Bradley B, Tian Geng, Lee Byung-Hoon, Shi Yanhong, Zhang Naixia, de Poot Stefanie A H, Tuebing Fabian, Sun Shuangwu, Vannoy Jacob, Tarasov Sergey G, Engen John R, Finley Daniel, Walters Kylie J
Abstract excerpt
Hundreds of pathways for degradation converge at ubiquitin recognition by a proteasome. Here, we found that the five known proteasomal ubiquitin receptors in yeast are collectively nonessential for ubiquitin recognition and identified a sixth receptor, Rpn1. A site ( T1: ) in the Rpn1 toroid recognized ubiquitin and ubiquitin-like ( UBL: ) domains of substrate shuttling factors. T1 structures with monoubiquitin...
Topics
- DNA-Binding Proteins
- Endopeptidases
- Metabolic Networks and Pathways
- Models, Molecular
- Mutation
- Proteasome Endopeptidase Complex
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins
- Ubiquitin-Specific Proteases
- Ubiquitination