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

Citation
R. De Mot et al., A self-compartmentalizing protease in Rhodococcus: the 20S proteasome, ANTON LEEUW, 74(1-3), 1998, pp. 83-87
Citations number
27
Categorie Soggetti
Microbiology
Journal title
ANTONIE VAN LEEUWENHOEK INTERNATIONAL JOURNAL OF GENERAL AND MOLECULAR MICROBIOLOGY
ISSN journal
00036072 → ACNP
Volume
74
Issue
1-3
Year of publication
1998
Pages
83 - 87
Database
ISI
SICI code
0003-6072(199807/10)74:1-3<83:ASPIRT>2.0.ZU;2-T
Abstract
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.