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Nature Structural & Molecular Biology 15, 218 - 220 (2008)
doi:10.1038/nsmb0308-218
Forging a proteasome 
-ring with dedicated proteasome chaperones
Rina Rosenzweig1 & Michael H Glickman1
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Rina Rosenzweig and Michael H. Glickman are in the Department of Biology, Technion-Israel Institute of Technology, Haifa 32000, Israel.
e-mail: glickman@tx.technion.ac.il
Abstract
Assembly of the 34-subunit, 2.5 megadalton 26S proteasome starts with formation of the seven-membered 
-ring. A set of newly identified proteasome chaperones serves as a clamp to seal -rings with the correct composition. By regulating the efficiency and outcome of this crucial step in proteasome biogenesis, these dedicated proteasome chaperones apparently partake in the stress response and in adaptation to intracellular proteolysis needs.
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