Forging a proteasome alpha-ring with dedicated proteasome chaperones

Rina Rosenzweig; Michael H. Glickman

doi:10.1038/nsmb0308-218

Forging a proteasome alpha-ring with dedicated proteasome chaperones

Rina Rosenzweig, Michael H. Glickman^*

^*Corresponding author for this work

Department of Chemical and Structural Biology

Research output: Contribution to journal › Editorial › peer-review

8 Citations (Scopus)

Abstract

Assembly of the 34- subunit, 2.5 megadalton 26S proteasome starts with formation of the seven-membered alpha-ring. A set of newly identified proteasome chaperones serves as a clamp to seal alpha-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 & Molecular Biology
Volume	15
Issue number	3
DOIs	https://doi.org/10.1038/nsmb0308-218
Publication status	Published - Mar 2008

All Science Journal Classification (ASJC) codes

Structural Biology
Molecular Biology

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10.1038/nsmb0308-218

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title = "Forging a proteasome alpha-ring with dedicated proteasome chaperones",

abstract = "Assembly of the 34- subunit, 2.5 megadalton 26S proteasome starts with formation of the seven-membered alpha-ring. A set of newly identified proteasome chaperones serves as a clamp to seal alpha-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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AB - Assembly of the 34- subunit, 2.5 megadalton 26S proteasome starts with formation of the seven-membered alpha-ring. A set of newly identified proteasome chaperones serves as a clamp to seal alpha-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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DO - 10.1038/nsmb0308-218

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EP - 220

JO - Nature Structural & Molecular Biology

JF - Nature Structural & Molecular Biology

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Forging a proteasome alpha-ring with dedicated proteasome chaperones

Abstract

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