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Cell biology

Destruction deconstructed

Nature volume 482, pages 170–171 (2012)Cite this article

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Correctly dismantling a structure can be as challenging as assembling it. The architecture of the yeast proteasome reveals this enzyme's intricate machinery for protein degradation. See Article p.186

The ensemble of proteins that makes up a cell is constantly changing. The malleability of a cell's protein content on a short timescale is largely due to the proteasome — a complex member of the protease family of enzymes, which break down proteins. The proteasome, found in eukaryotic organisms (such as plants, animals and yeast), is composed of two main parts: the 20S core particle, which is a 28-subunit protein-destruction complex, and the 19S regulatory particle, a 19-subunit complex that mediates substrate selection. On page 186 of this issue, Lander et al.1 report the complete subunit structure of the yeast 19S regulatory particle. The results include many surprises and some puzzles that will challenge the proteasome field.

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Figure 1: The evolution of proteases.
Figure 2: Subunit architecture of the yeast proteasome regulatory particle1.

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Authors and Affiliations

  1. Geng Tian and Daniel Finley are in the Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.,

    Geng Tian & Daniel Finley

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  1. Geng Tian
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  2. Daniel Finley
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Correspondence to Daniel Finley.

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Tian, G., Finley, D. Destruction deconstructed. Nature 482, 170–171 (2012). https://doi.org/10.1038/482170a

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