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The Proteasome — Ubiquitin Protein Degradation Pathway pp 73–89Cite as

The 11S Regulators of 20S Proteasome Activity

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Part of the book series: Current Topics in Microbiology and Immunology ((CT MICROBIOLOGY,volume 268))

Abstract

The 20S proteasome, an approximately 700-kDa complex of 28 protein subunits, performs most of the proteolysis that takes place in the cytosol and nucleus of eukaryotic cells. As discussed elsewhere in this volume, structural studies on the 20S proteasome revealed that the active sites are sequestered within a central catalytic chamber that substrates access by passing through a narrow opening (α annulus) (Groll et al. 1997; Löwe et al. 1995; Wenzel and Baumeister 1995). This architecture explains how the 20S proteasome, which is an abundant and nonspecific protease, avoids unregulated degradation of inappropriate substrates. Because the α annulus is normally closed by N-terminal sequences of the 20S proteasome α subunits, this architecture also appears to restrict the release of degradation products from the proteasome interior.

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  1. Biochemistry Department, University of Utah Medical School, 50 N Medical Drive, 84132, Salt Lake City, Utah, USA

    C. P. Hill, E. I. Masters & F. G. Whitby

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  2. E. I. Masters
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  1. Department of Molecular Structural Biology, Max-Planck-Institute for Biochemistry, Am Klopferspit 18 a, 82152, Martinsried, Germany

    Peter Zwickl  & Wolfgang Baumeister  & 

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Hill, C.P., Masters, E.I., Whitby, F.G. (2002). The 11S Regulators of 20S Proteasome Activity. In: Zwickl, P., Baumeister, W. (eds) The Proteasome — Ubiquitin Protein Degradation Pathway. Current Topics in Microbiology and Immunology, vol 268. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-59414-4_4

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