1. The metalloprotease of Listeria monocytogenes is activated by intramolecular autocatalysis
- Author
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Bitar, Alan Pavinski, Cao, Min, and Marquis, Helene
- Subjects
Listeria monocytogenes -- Physiological aspects ,Proteases -- Physiological aspects ,Organometallic compounds -- Physiological aspects ,Biological sciences - Abstract
The metalloprotease (Mpl) of Listeria monocytogenes is a thermolysin-like protease that mediates the maturation of a broad-range phospholipase C, whose function contributes to the ability of this food-borne bacterial pathogen to survive intracellularly. Mpl is made as a proprotein that undergoes maturation by proteolytic cleavage of a large N-terminal prodomain. In this study, we identified the N terminus of mature Mpl and generated Mpl catalytic mutants to investigate the mechanism of Mpl maturation. We observed that Mpl activity was a prerequisite for maturation, suggesting a mechanism of autocatalysis. Furthermore, using a strain of L. monocytogenes expressing both the wild-type form and a catalytic mutant form of Mpl simultaneously, we determined that in vivo maturation of Mpl occurs exclusively by an intramolecular autocatalysis mechanism.
- Published
- 2008