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Intracellular Protein Catabolism pp 187–195Cite as

Protein and Gene Structures of 20S and 26S Proteasomes

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 389))

Abstract

The two types of proteasomes with apparent sedimentation coefficients of 20S and 26S consist of a number of heterogeneous polypeptides and are unusually large protein complexes of approximately 750 kDa and 2000 kDa, respectively. The 26S proteasome is a cylindrical caterpillar-shaped complex with a symmetrical assembly of a four-layered central 20S proteasome and two terminal 22S regulators each with a V-like structure. The central core and the terminal structures are formed by multiple polypeptides with molecular masses of 21–31 kDa and 28–112 kDa, respectively. We have been studying their detailed structures by protein-chemical and molecular biological techniques. In this review, we summarize the structural features of eukaryotic 20S and 26S proteasomes. We also discuss the possible function(s) of the terminal multi-protein regulator complex based on current information.

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Author information

Authors and Affiliations

  1. Institute for Enzyme Research, University of Tokushima, 770, Tokushima, Japan

    Keiji Tanaka, Tomohiro Tamura, Nobuyuki Tanahashi & Chizuko Tsurumi

Authors
  1. Keiji Tanaka
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  2. Tomohiro Tamura
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  3. Nobuyuki Tanahashi
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  4. Chizuko Tsurumi
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Editor information

Editors and Affiliations

  1. University of Tokyo, Tokyo, Japan

    Koichi Suzuki

  2. College of Medicine, Penn State University, Hershey, Pennsylvania, USA

    Judith S. Bond

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© 1996 Plenum Press, New York

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Tanaka, K., Tamura, T., Tanahashi, N., Tsurumi, C. (1996). Protein and Gene Structures of 20S and 26S Proteasomes. In: Suzuki, K., Bond, J.S. (eds) Intracellular Protein Catabolism. Advances in Experimental Medicine and Biology, vol 389. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0335-0_23

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  • DOI: https://doi.org/10.1007/978-1-4613-0335-0_23

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-8003-0

  • Online ISBN: 978-1-4613-0335-0

  • eBook Packages: Springer Book Archive

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