Forging a proteasome α-ring with dedicated proteasome chaperones

Rina Rosenzweig; Michael Glickman

doi:10.1038/nsmb0308-218

Forging a proteasome α-ring with dedicated proteasome chaperones

Research output: Contribution to journal › Short survey › peer-review

Abstract

Assembly of the 34-subunit, 2.5 megadalton 26S proteasome starts with formation of the seven-membered α-ring. A set of newly identified proteasome chaperones serves as a clamp to seal α-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.

Original language	English
Pages (from-to)	218-220
Number of pages	3
Journal	Nature Structural and Molecular Biology
Volume	15
Issue number	3
DOIs	https://doi.org/10.1038/nsmb0308-218
State	Published - Mar 2008

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1038/nsmb0308-218

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Forging a proteasome α-ring with dedicated proteasome chaperones

Abstract

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