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Review
. 2009 Feb;10(2):104-15.
doi: 10.1038/nrm2630.

Molecular mechanisms of proteasome assembly

Shigeo Murata  1 , Hideki Yashiroda, Keiji Tanaka
Affiliations
Review

Molecular mechanisms of proteasome assembly

Shigeo Murata et al. Nat Rev Mol Cell Biol. 2009 Feb.

Abstract

The 26S proteasome is a highly conserved protein degradation machine that consists of the 20S proteasome and 19S regulatory particles, which include 14 and 19 different polypeptides, respectively. How the proteasome components are assembled is a fundamental question towards understanding the process of protein degradation and its functions in diverse biological processes. Several proteasome-dedicated chaperones are involved in the efficient and correct assembly of the 20S proteasome. These chaperones help the initiation and progression of the assembly process by transiently associating with proteasome precursors. By contrast, little is known about the assembly of the 19S regulatory particles, but several hints have emerged.

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