Assembly of the 34-subunit, 2.5 MDa 26S proteasome is a carefully choreographed intricate process. It starts with formation of a seven-membered α-ring that serves as a template for assembly of the complementary β-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.
Conference Article| September 19 2008
Chaperone-driven proteasome assembly
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Rina Rosenzweig, Michael H. Glickman; Chaperone-driven proteasome assembly. Biochem Soc Trans 1 October 2008; 36 (5): 807–812. doi: https://doi.org/10.1042/BST0360807
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