Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


          Institute: MPI für Biochemie     Collection: Structural Biology (W. Baumeister)     Display Documents



ID: 318324.0, MPI für Biochemie / Structural Biology (W. Baumeister)
A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the cop9-signalosome and eif3
Authors:Glickman, M. H.; Rubin, D. M.; Coux, O.; Wefes, I.; Pfeifer, G.; Cjeka, Z.; Baumeister, W.; Fried, V. A.; Finley, D.
Date of Publication (YYYY-MM-DD):1998-09-04
Title of Journal:Cell
Volume:94
Issue / Number:5
Start Page:615
End Page:623
Audience:Not Specified
Abstract / Description:The proteasome consists of a 20S proteolytic core particle (CP) and a 19S regulatory particle (RP), which selects ubiquitinated substrates for translocation into the CP. An eight-subunit subcomplex of the RP, the lid, can be dissociated from proteasomes prepared from a deletion mutant for Rpn10, an RP subunit. A second subcomplex, the base, contains all six proteasomal ATPases and links the RP to the CP. The base is sufficient to activate the CP for degradation of peptides or a nonubiquitinated protein, whereas the lid is required for ubiquitin-dependent degradation. By electron microscopy, the base and the lid correspond to the proximal and distal masses of the RP, respectively. The lid subunits share sequence motifs with components of the COPS/signalosome complex and eIF3, suggesting that these functionally diverse particles have a common evolutionary ancestry. [References: 47]
Free Keywords:Initiation-factor eif3; 20s proteasome; Multicatalytic protease; Dependent proteases; 20-s proteasome; 11-s regulator; Subunits; Complex; Yeast; Purification.; Cell & developmental biology.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.