Format

Send to

Choose Destination
See comment in PubMed Commons below
Biochem Soc Trans. 2008 Oct;36(Pt 5):807-12. doi: 10.1042/BST0360807.

Chaperone-driven proteasome assembly.

Author information

1
Department of Biology, Technion - Israel Institute of Technology, 32000 Haifa, Israel.

Abstract

Assembly of the 34-subunit, 2.5 MDa 26S proteasome is a carefully choreographed intricate process. It starts with formation of a seven-membered alpha-ring that serves as a template for assembly of the complementary beta-ring-forming 'half-proteasomes'. Dimerization results in a latent 20S core particle that can serve further as a platform for 19S regulatory particle attachment and formation of the biologically active 26S proteasome for ubiquitin-dependent proteolysis. Both general and dedicated proteasome assembly chaperones regulate the efficiency and outcome of critical steps in proteasome biogenesis, and in complex association.

PMID:
18793141
DOI:
10.1042/BST0360807
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire
    Loading ...
    Support Center