Protease inhibitors in bacteria: an emerging concept for the regulation of bacterial protein complexes?
Serine protease inhibitors (serpins), the antagonists of serine proteases, were unknown in the bacterial kingdom until recently. Kang et al. in this issue of Molecular Microbiology report the cloning and functional analysis of the three serpin genes from the thermophilic anaerobic bacterium Clostridium thermocellum. Two of the serpins contain a dockerin module for location in the extracellular hydrolytic multienzyme complex, the cellulosome. The susceptibility of cellulosome to proteolytic degradation and the presence of a serine protease in the same complex provoke speculation that protease inhibitor/protease pairs could play hitherto unrecognized roles in protein stability and regulation in bacteria.
Schwarz
Wolfgang H
WH
Institute for Microbiology, Technische Universität München, Am Hochanger 4, D-85350 Freising-Weihenstephan, Germany. wschwarz@wzw.tum.de
Zverlov
Vladimir V
VV
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D048013:Acetivibrio thermocellus / Q000235:genetics / Q000378:metabolism*; D005798:Genes, Bacterial; D015842:Serine Proteinase Inhibitors / Q000235:genetics / Q000378:metabolism*; D015843:Serpins / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; D015842:Serine Proteinase Inhibitors; D015843:Serpins