The metalloprotease of Listeria monocytogenes is activated by intramolecular autocatalysis

Journal of Bacteriology

Volumn 190, Issue 1, 2008, Pages 107-111

  Bitar, Alan Pavinski ^a   Cao, Min ^a,b   Marquis, Hélène ^a  

^a Cornell University ^*  (United States)

^b CLEMSON UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

METALLOPROTEINASE; MUTANT PROTEIN; PHOSPHOLIPASE C; THERMOLYSIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME MECHANISM; LISTERIA MONOCYTOGENES; NONHUMAN; PRIORITY JOURNAL; WILD TYPE;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CATALYSIS; DNA PRIMERS; ENZYME ACTIVATION; GENOTYPE; KINETICS; LISTERIA MONOCYTOGENES; METALLOPROTEASES; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; RECOMBINANT PROTEINS; TYPE C PHOSPHOLIPASES;

BACTERIA (MICROORGANISMS); LISTERIA MONOCYTOGENES;

EID: 37549035018     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00852-07     Document Type: Article

References (30)

1. Ahmed, S. A., P. McPhie, and L. A. Smith. 2003. Autocatalytically fragmented light chain of botulinum a neurotoxin is enzymatically active. Biochemistry 42:12539-12549.
2. Banbula, A., J. Potempa, J. Travis, C. Fernandez-Catalan, K. Mann, R. Huber, W. Bode, and F. Medrano. 1998. Amino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 A resolution. Structure 6:1185-1193.
3. Beaumont, A., M. J. O'Donohue, N. Paredes, N. Rousselet, M. Assicot, C. Bohuon, M. C. Fournie-Zaluski, and B. P. Roques. 1995. The role of histidine 231 in thermolysin-like enzymes. A site-directed mutagenesis study. J. Biol. Chem. 270:16803-16808.
4. Bishop, D. K., and D. J. Hinrichs. 1987. Adoptive transfer of immunity to Listeria monocytogenes: the influence of in vitro stimulation on lymphocyte subset requirements. J. Immunol. 139:2005-2009.
5. Camilli, A., L. G. Tilney, and D. A. Portnoy. 1993. Dual roles of plcA in Listeria monocytogenes pathogenesis. Mol. Microbiol. 8:143-157.
6. Domann, E., M. Leimeister-Wächter, W. Goebel, and T. Chakraborty. 1991. Molecular cloning, sequencing, and identification of a metalloprotease gene from Listeria monocytogenes that is species specific and physically linked to the listeriolysin gene. Infect. Immun. 59:65-72.
7. Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
8. Holmes, M. A., and B. W. Matthews. 1982. Structure of thermolysin refined at 1.6 A resolution. J. Mol. Biol. 160:623-639.
9. Hu, Z., K. Haghjoo, and F. Jordan. 1996. Further evidence for the structure of the subtilisin propeptide and for its interactions with mature subtilisin. J. Biol. Chem. 271:3375-3384.
10. Kawamoto, S., Y. Shibano, J. Fukushima, N. Ishii, K. Morihara, and K. Okuda. 1993. Site-directed mutagenesis of Glu-141 and His-223 in Pseudomonas aeruginosa elastase: catalytic activity, processing, and protective activity of the elastase against Pseudomonas infection. Infect. Immun. 61:1400-1405.
11. Kooi, C., C. R. Corbett, and P. A. Sokol. 2005. Functional analysis of the Burkholderia cenocepacia ZmpA metalloprotease. J. Bacteriol. 187:4421-4429.
12. Lauer, P., M. Y. N. Chow, M. J. Loessner, D. A. Portnoy, and R. Calendar. 2002. Construction, characterization, and use of two Listeria monocytogenes site-specific phage integration vectors. J. Bacteriol. 184:4177-4186.
13. Marie-Claire, C., B. P. Roques, and A. Beaumont. 1998. Intramolecular processing of prothermolysin. J. Biol. Chem. 273:5697- 5701.
14. Marquis, H., V. Doshi, and D. A. Portnoy. 1995. The broad-range phospholipase C and a metalloprotease mediate listeriolysin O-independent escape of Listeria monocytogenes from a primary vacuole in human epithelial cells. Infect. Immun. 63:4531-4534.
15. Marquis, H., H. Goldfine, and D. A. Portnoy. 1997. Proteolytic pathways of activation and degradation of a bacterial phospholipase C during intracellular infection by Listeria monocytogenes. J. Cell Biol. 137:1381-1392.
16. McIver, K., E. Kessler, and D. E. Ohman. 1991. Substitution of active-site His-223 in Pseudomonas aeruginosa elastase and expression of the mutated lasB alleles in Escherichia coli show evidence for autoproteolytic processing of proelastase. J. Bacteriol. 173:7781-7789.
17. McIver, K. S., E. Kessler, J. C. Olson, and D. E. Ohman. 1995. The elastase propeptide functions as an intramolecular chaperone required for elastase activity and secretion in Pseudomonas aeruginosa. Mol. Microbiol. 18:877-889.
18. Menard, R., E. Carmona, S. Takebe, E. Dufour, C. Plouffe, P. Mason, and J. S. Mort. 1998. Autocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro. J. Biol. Chem. 273:4478-4484.
19. Mengaud, J., C. Geoffroy, and P. Cossart. 1991. Identification of a new operon involved in Listeria monocytogenes virulence: its first gene encodes a protein homologous to bacterial metalloproteases. Infect. Immun. 59:1043-1049.
20. Miyoshi, S., and S. Shinoda. 2000. Microbial metalloproteases and pathogenesis. Microbes Infect. 2:91-98.
21. Poyart, C., E. Abachin, I. Razafimanantsoa, and P. Berche. 1993. The zinc metalloprotease of Listeria monocytogenes is required for maturation of phosphatidylcholine phospholipase C: direct evidence obtained by gene complementation. Infect. Immun. 61:1576-1580.
22. Shetron-Rama, L. M., K. Mueller, J. M. Bravo, H. G. Bouwer, S. S. Way, and N. E. Freitag. 2003. Isolation of Listeria monocytogenes mutants with high-level in vitro expression of host cytosol-induced gene products. Mol. Microbiol. 48:1537-1551.
23. Shinde, U., and M. Inouye. 2000. Intramolecular chaperones: polypeptide extensions that modulate protein folding. Semin. Cell Dev. Biol. 11:35-44.
24. Smith, G. A., H. Marquis, S. Jones, N. C. Johnston, D. A. Portnoy, and H. Goldfine. 1995. The two distinct phospholipases C of Listeria monocytogenes have overlapping roles in escape from a vacuole and cell-to-cell spread. Infect. Immun. 63:4231-4237.
25. Snyder, A., and H. Marquis. 2003. Restricted translocation across the cell wall regulates secretion of the broad-range phospholipase C of Listeria monocytogenes. J. Bacteriol. 185:5953-5958.
26. Tilney, L. G., and D. A. Portnoy. 1989. Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes. J. Cell Biol. 109:1597-1608.
27. Van Wart, H. E., and H. Birkedal-Hansen. 1990. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl. Acad. Sci. USA 87:5578-5582.
28. Vazquez-Boland, J.-A., C. Kocks, S. Dramsi, H. Ohayon, C. Geoffroy, J. Mengaud, and P. Cossart. 1992. Nucleotide sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread. Infect. Immun. 60:219-230.
29. Wetmore, D. R., S. L. Wong, and R. S. Roche. 1992. The role of the prosequence in the processing and secretion of the thermolysin-like neutral protease from Bacillus cereus. Mol. Microbiol. 6:1593-1604.
30. Yeung, P. S., N. Zagorski, and H. Marquis. 2005. The metalloprotease of Listeria monocytogenes controls cell wall translocation of the broad-range phospholipase C. J. Bacteriol. 187:2601-2608.