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Journal of Bacteriology, January 2008, p. 107-111, Vol. 190, No. 1
0021-9193/08/$08.00+0 doi:10.1128/JB.00852-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.
,
and
Hélène Marquis*
Department of Microbiology and Immunology, Cornell University, Ithaca, New York 14853
Received 1 June 2007/ Accepted 15 October 2007
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 ahead of print on 26 October 2007.
Supplemental material for this article may be found at http://jb.asm.org/.
Present address: Department of Biological Sciences, Clemson University, Clemson, SC 29634.
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