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Forging a proteasome α-ring with dedicated proteasome chaperones

Nature Structural & Molecular Biology volume 15, pages 218–220 (2008)Cite this article

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.

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Figure 1: Chaperone-facilitated eukaryotic proteasome assembly.
Figure 2: The α-ring as a template for the stacked 20S barrel.
Figure 3: Pba3–Pba4 as an α-ring clamp.

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Authors and Affiliations

  1. Rina Rosenzweig and Michael H. Glickman are in the Department of Biology, Technion-Israel Institute of Technology, Haifa 32000, Israel. glickman@tx.technion.ac.il,

    Rina Rosenzweig & Michael H Glickman

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  1. Rina Rosenzweig
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  2. Michael H Glickman
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Rosenzweig, R., Glickman, M. Forging a proteasome α-ring with dedicated proteasome chaperones. Nat Struct Mol Biol 15, 218–220 (2008). https://doi.org/10.1038/nsmb0308-218

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