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

Antonie Van Leeuwenhoek. 1998 Jul-Oct;74(1-3):83-7. doi: 10.1023/a:1001708012708.

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.

Publication types

  • Review

MeSH terms

  • Adenosine Triphosphatases* / classification
  • Adenosine Triphosphatases* / genetics
  • Adenosine Triphosphatases* / ultrastructure
  • Bacteria / enzymology
  • Cell Compartmentation
  • Cysteine Endopeptidases* / classification
  • Cysteine Endopeptidases* / genetics
  • Cysteine Endopeptidases* / ultrastructure
  • Multienzyme Complexes* / classification
  • Multienzyme Complexes* / genetics
  • Multienzyme Complexes* / ultrastructure
  • Proteasome Endopeptidase Complex
  • Protein Conformation
  • Rhodococcus / enzymology*

Substances

  • Multienzyme Complexes
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex
  • Adenosine Triphosphatases