Jul 1, 1995

The first characterization of a eubacterial proteasome: the 20S complex of Rhodococcus

Current Biology : CB
T TamuraW Baumeister

Abstract

The 26S proteasome is the central protease of the ubiquitin-dependent pathway of protein degradation. The proteolytic core of the complex is formed by the 20S proteasome, a cylinder-shaped particle that in archaebacteria contains two different subunits (alpha and beta) and in eukaryotes contains fourteen different subunits (seven of the alpha-type and seven of the beta-type). We have purified a 20S proteasome complex from the nocardioform actinomycete Rhodococcus sp. strain NI86/21. The complex has an apparent relative molecular mass of 690 kD, and efficiently degrades the chymotryptic substrate Suc-Leu-Leu-Val-Tyr-AMC in the presence or absence of 0.05% SDS. Purified preparations reveal the existence of four subunits, two of the alpha-type and two of the beta-type, the genes for which we have cloned and sequenced. Electron micrographs show that the complex has the four-ringed, cylinder-shaped appearance typical of proteasomes. The recent description of the first eubacterial ubiquitin, and our discovery of a eubacterial proteasome show that the ubiquitin pathway of protein degradation is ancestral and common to all forms of life.

  • References23
  • Citations80

References

  • References23
  • Citations80

Citations

Mentioned in this Paper

Biochemical Pathway
Proteasome Pathway
Protein Degradation, Regulatory
RSU26421
Ubiquitin
Protein Degradation, Metabolic
Homologous Sequences, Amino Acid
Archaea
Endopeptidases
Proteolytic Enzyme

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