Specific inhibition of mature fungal serine proteinases and metalloproteinases by their propeptides

Journal of Bacteriology

Volumn 178, Issue 8, 1996, Pages 2211-2215

  Markaryan, Adam ^a   Lee, J D ^a   Sirakova, Tatiana D ^a   Kolattukudy, P E ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

METALLOPROTEINASE; PROTEIN PRECURSOR; SERINE PROTEINASE;

ARTICLE; ASPERGILLUS FUMIGATUS; ENZYME INHIBITION; ENZYME RELEASE; ENZYME SYNTHESIS; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION;

ASPERGILLUS FLAVUS; ASPERGILLUS FUMIGATUS; ESCHERICHIA; ESCHERICHIA COLI;

EID: 0029930574     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.8.2211-2215.1996     Document Type: Article

References (35)

1. Baker, D., A. K. Shiau, and D. A. Agard. 1993. The role of pro regions in protein folding Curr. Opin. Cell Biol. 5:966-970.
2. Baker, D., J. L. Silen, and D. A. Agard. 1992. Protease pro region required for folding is a potent inhibitor of the mature enzyme. Proteins Struct. Funct. Genet. 12:339-344.
3. Baker, D., J. L. Silen, and D. A. Agard. 1992. A protein-folding reaction under kinetic control. Nature (London) 356:263-265.
4. Bieth, J. 1974. Some kinetic consequences of the tight binding of protein proteinase inhibitors to proteolytic enzyme and their application to the determination of dissociation constants, p 463-469. In Bayer Symposium V: Proteinase inhibitors. Springer-Verlag, Berlin.
5. Bochkareva, E. S., N. M. Lissin, and A. S. Girschovich. 1988. Transient association of newly synthesized unfolded proteins with the heat shock Gro EL protein Nature (London) 336:254-257
6. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72:248-254.
7. 6a. Bryan, P., L. Wang, J. Hoskins, S. Ruvinov, S. Strausberg, P. Alexander, O. Almog, G. Gilliland, and T. Gallagher. 1995 Catalysis of a protein folding reaction: mechanistic implications of the 2.0Å structure of the subtilisin-prodomain complex Biochemistry 32:8112-8119.
8. Chang, S. C., P. C. Chang, and Y.-H. W. Lee. 1994. The roles of propeptide in maturation and secretion of Npr protease from Streptomyces J. Biol. Chem. 269:3548-3554.
9. Fabre, E., C. Tharaud, and C. Gaillardin. 1994. Intracellular transit of a yeast protease is rescued by trans-complementation with its prodomain. J. Biol. Chem. 267:15049-15055.
10. Fox, T., E. De Miguel, J. S. Mort, and A. C. Storer. 1992. Potent slow-binding inhibition of cathepsin B by its propeptide. Biochemistry 31:12571-12576.
11. Frederick, G. D., P. Rombouts, and F. P. Buxton. 1993. Cloning and characterization of pepC, a gene encoding a serine proteinase from Aspergillus niger. Gene 125:57-64.
12. Fusek, M., M. Mares, J. Vagner, Z. Voburka, and M. Baudys. 1991. Inhibition of aspartic proteinases by propart peptides of human procathepsin D and chicken pepsinogen. FEBS Lett. 287:160-162.
13. Ikemura, H., H. Takagi, and M. Inouye. 1987 Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli. J. Biol. Chem 262:7359-7864
14. Jarai, G., D. Kirchherr, and F. P. Buxton. 1994 Cloning and characterization of the pepD gene of Aspergillus niger which codes for a subtilism-like protease. Gene 139:51-57.
15. Jaton-Ogay, K., S. Paris, M. Huerre, M. Quadroni, R. Falchetto, G. Togni, J.-P. Latge, and M. Mono. 1994. Cloning and disruption of the gene encoding an extracellular metalloproteinase of Aspergillus fumegatus. Mol. Microbiol. 4:917-928
16. Jaton-Ogay, K., M. Suter, R. Crameri, R. Falchetto, A. Fatih, and M. Mono. 1992. Nucleotide sequence of a genomic and cDNA clone encoding an extracellular alkaline protease of Aspergillus fumigatus. FEMS Microbiol. Lett 92:163-168.
17. 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 elaxtase: catalytic activity, processing, and protective activity of the elastase against Pseudomonas infection. Infect. Immun. 61:1400-1405.
18. Kessler, E., and M. Safrin. 1994 The propeptide of Pseudomonas aeruginosa elastase acts as an elastase inhibitor. J. Biol. Chem. 269:22726-22731.
19. Kolattukudy, P. E., J. D. Lee, L. M. Rogers, P. Zimmerman, S. Ceselski, B. Fox, B. Stein, and E. A. Copelan. 1993. Evidence for possible involvement of an elastolytic serine protease in aspergillosis Infect. Immun 61:2357-2368.
20. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
21. Lee, J. D., and P. E. Kolattukudy. 1995. Molecular cloning of the cDNA and gene for an elastinolytic aspartic proteinase from Aspergillus fumigatus and evidence of its secretion by the fungus during invasion of the host lung. Infect. Immun. 63:3796-3803.
22. Markaryan, A., I. Morozova, H. Yu, and P. E. Kolattukudy. 1994. Purification and characterization of an elastinolytic metalloproteinase from Aspergillus fumigatus and immunoelectron microscopic evidence of secretion of this enzyme by the fungus invading the murine lung Infect Immun. 62:2149-2157.
23. 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 in Escherichia coli show evidence for autoproteolytic processing of proelastase. J. Bacteriol. 173:7781-7789
24. Oda, K., T. Koyama, and S. Murao. 1979 Purification and properties of a proteinaceous metallo-proteinase inhibitor from Streptomyces nigrescens TK-23. Biochim Biophys. Acta 571:147-156.
25. Ohta, Y., H. Hojo, S. Aimoto, T. Kobayashi, X. Zhu, F. Jordan, and M. Inouye. 1991. Pro-peptide as an intramolecular chaperone renaturation of denatured subtilisin E with a synthetic propeptide. Mol. Microbiol. 5:1506-1510.
26. Ramesh, M. V., T. D. Sirakova, and P. E. Kolattukudy. 1994. Isolation, characterization, and cloning of cDNA and the gene for an elastinolytic serine proteinase from Aspergillus flavus. Infect. Immun. 62:79-85.
27. Ramesh, M. V., T. D. Sirakova, and P. E. Kolattukudy. 1995. Cloning and characterization of the cDNAs and genes (mep20) encoding homologous metalloproteases from Aspergillus flavus and A. fumigatus. Gene 165:121-125.
28. SanSegunido, B. S., M. C. Martinez, M. Vilanova, C. M. Cuchille, and F. X. Aviles. 1982, The severed activation segment of porcine pancreatic procarboxypeptidase A is a powerful inhibitor of the active enzyme Biochim. Biophys. Acta 707:74-80.
29. Shinde, U., Y. Li, S. Chatterjee, and M. Inouye. 1993. Folding pathway mediated by an intramolecular chaperone. Proc. Natl. Acad. Sci. USA 90:6924-6928.
30. Silen, J. L., and D. A. Agard. 1989. The α-lytic protease pro-region does not require a physical linkage to activate the protease domain in vitro Nature (London) 341:462-464.
31. Silen, J. L., D. Frank, A. Fujishige, R. Bone, and D. A. Agard. 1989. Analysis of prepro-α-lytic protease expression in Escherichia coli reveals that the pro region is required for activity. J. Bacteriol. 171:1320-1325.
32. Silen, R. A., C. N. McGrath, K. R. Smith, and D. A. Agard. 1988 Molecular analysis of the gene encoding alpha-lytic protease: evidence for a preproenzyme. Gene 69:237-244.
33. Sirakova, T. D., A. Markaryan, and P. E. Kolattukudy. 1994 Molecular cloning and sequencing of the cDNA and gene for a novel elastinolytic metalloproteinase from Aspergillus fumigatus and its expression in Escherichia coli Infect. Immun. 62:79-85.
34. Tatsumi, H., S. Murakami, R. F. Tsuji, Y. Ishida, K. Murakami, A. Masaki, H. Kawabe, H. Arimura, E. Nakano, and H. Motai. 1991. Cloning and expression in yeast of a cDNA clone encoding Aspergillus oryzae neutral protease II, a unique metalloprotease. Mol. Gen Genet. 228:97-103
35. Zhu, X., Y. Ohta, F. Jordan, and M. Inouye. 1989 Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process. Nature (London) 339:483-484.