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