Nature Communications (Oct 2021)
The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag
- Indrajit Sahu,
- Sachitanand M. Mali,
- Prasad Sulkshane,
- Cong Xu,
- Andrey Rozenberg,
- Roni Morag,
- Manisha Priyadarsini Sahoo,
- Sumeet K. Singh,
- Zhanyu Ding,
- Yifan Wang,
- Sharleen Day,
- Yao Cong,
- Oded Kleifeld,
- Ashraf Brik,
- Michael H. Glickman
Affiliations
- Indrajit Sahu
- Faculty of Biology, Technion–Israel Institute of Technology
- Sachitanand M. Mali
- Schulich faculty of Chemistry, Technion–Israel Institute of Technology
- Prasad Sulkshane
- Faculty of Biology, Technion–Israel Institute of Technology
- Cong Xu
- State Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences
- Andrey Rozenberg
- Faculty of Biology, Technion–Israel Institute of Technology
- Roni Morag
- Faculty of Biology, Technion–Israel Institute of Technology
- Manisha Priyadarsini Sahoo
- Faculty of Biology, Technion–Israel Institute of Technology
- Sumeet K. Singh
- Schulich faculty of Chemistry, Technion–Israel Institute of Technology
- Zhanyu Ding
- State Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences
- Yifan Wang
- State Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences
- Sharleen Day
- Department of Medicine, Perelman School of Medicine, University of Pennsylvania
- Yao Cong
- State Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences
- Oded Kleifeld
- Faculty of Biology, Technion–Israel Institute of Technology
- Ashraf Brik
- Schulich faculty of Chemistry, Technion–Israel Institute of Technology
- Michael H. Glickman
- Faculty of Biology, Technion–Israel Institute of Technology
- DOI
- https://doi.org/10.1038/s41467-021-26427-0
- Journal volume & issue
-
Vol. 12,
no. 1
pp. 1 – 21
Abstract
The 20S particle is part of the 26S proteasome, but also exists as a free complex. Here, the authors outline signature activities of the 20S and combine chemical, structural, functional and proteomic assays to show that the 20S can degrade ubiquitin tags along with conjugated substrates.
