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The 20 S Proteasome

  • Chapter
Ubiquitin and the Biology of the Cell

Abstract

The 26 S proteasome—discussed in Chapter 6—is the central protease of the ubiquitin pathway of protein degradation. The core of this 2-MDa enzyme is formed by the 20 S proteasome (Peters et al., 1993), a barrel-shaped protease of about 700 kDa, which is the subject of this chapter (Fig. 1). Whereas the 26 S proteasome degrades folded proteins in an ATP-dependent manner, the 20 S proteasome is ATP-independent and only degrades entirely unfolded polypeptides.

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Authors and Affiliations

  1. Molekulare Strukturbiologie, Max-Planck-Institute für Biochemie, D-82152, Martinsried, Germany

    Andrei Lupas & Wolfgang Baumeister

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  1. Andrei Lupas
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  2. Wolfgang Baumeister
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Editors and Affiliations

  1. Research Institute of Molecular Pathology, Vienna, Austria

    Jan-Michael Peters

  2. Institute of Zoology, University of Mainz, Mainz, Germany

    J. Robin Harris

  3. Harvard Medical School, Boston, Massachusetts, USA

    Daniel Finley

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Lupas, A., Baumeister, W. (1998). The 20 S Proteasome. In: Peters, JM., Harris, J.R., Finley, D. (eds) Ubiquitin and the Biology of the Cell. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1922-9_5

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  • DOI: https://doi.org/10.1007/978-1-4899-1922-9_5

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