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A self-compartmentalizing protease in Rhodococcus: the 20S proteasome

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Abstract

The 26S proteasome represents a major, energy-dependent and self- compartmentalizing protease system in eukaryotes. The proteolytic core of this complex, the 20S proteasome, is also ubiquitous in archaea. Although absent from most eubacteria, this multi- subunit protease was recently discovered in Rhodococcus and appears to be confined to actinomycetes. The eubacterial 20S proteasome represents an attractive complementary system to study proteasome assembly, quaternary structure, and catalytic mechanism. In addition, it is likely to contribute substantially to our understanding of the role of various self-compartmentalizing proteases in bacterial cells.

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Authors and Affiliations

  1. F.A. Janssens Laboratory of Genetics, Catholic University of Leuven, Kardinaal Mercierlaan 92, B-3001, Heverlee, Belgium

    René De Mot & István Nagy

  2. Abteilung für Molekulare Strukturbiologie, Max-Planck- Institut für Biochemie, Martinsried, Germany

    Wolfgang Baumeister

Authors
  1. René De Mot
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  2. István Nagy
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  3. Wolfgang Baumeister
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Correspondence to Wolfgang Baumeister.

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De Mot, R., Nagy, I. & Baumeister, W. A self-compartmentalizing protease in Rhodococcus: the 20S proteasome. Antonie Van Leeuwenhoek 74, 83–87 (1998). https://doi.org/10.1023/A:1001708012708

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