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A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3
Author(s): Glickman MH, Rubin DM, Coux O, Wefes I, Pfeifer G, Cjeka Z, Baumeister W, Fried VA, Finley D
Source: CELL    Volume: 94    Issue: 5    Pages: 615-623    Published: SEP 4 1998  
Times Cited: 442     References: 47     
Abstract: 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.
Document Type: Article
Language: English
Reprint Address: Finley, D (reprint author), Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA
Addresses:
1. Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA
2. New York Med Coll, Dept Cell Biol, Valhalla, NY 10595 USA
3. Max Planck Inst Biochem, D-82152 Martinsried, Germany
Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138 USA
Subject Category: Biochemistry & Molecular Biology; Cell Biology
IDS Number: 118QR
ISSN: 0092-8674
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