1887

Abstract

Summary: produces an 82 kDa intracellular metalloproteinase that hydrolyses the Pz-peptide, 4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-Arg, a typical substrate of members of the thimet oligopeptidase family which is ubiquitously distributed across animal species. The gene encoding this 82 kDa metalloproteinase was cloned and sequenced. Analysis of the deduced amino acid sequence of showed that the MepB protein is a cytosolic zinc metalloproteinase of the thimet oligopeptidase family (M3) and as such is probably involved in the intracellular degradation of small peptides. An mutant that lacks the MepB Pz-peptidolytic activity was constructed by gene disruption at the locus. Analysis of this mutant did not reveal any detectable phenotype.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-143-7-2247
1997-07-01
2024-12-12
Loading full text...

Full text loading...

/deliver/fulltext/micro/143/7/mic-143-7-2247.html?itemId=/content/journal/micro/10.1099/00221287-143-7-2247&mimeType=html&fmt=ahah

References

  1. Ausubel F. M., Brent R., Kingston R. E., Moore D. D., Seidman J. G., Smith J. A., Struhl K. 1992 Short Protocols in Molecular Biology New York: John Wiley;
    [Google Scholar]
  2. Barrett A. J., Brown M. A., Dando P. M., Knight C. G., McKie N., Rawlings N. D., Serizawa A. 1995; Thimet oligopeptidase and oligopeptidase M or neurolysin. Methods Enzymol 248:529–556
    [Google Scholar]
  3. Bode W., Gomis-Rüth F. W., Stöckler W. 1993; Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the ‘metzincins’. FEBS Lett 331:134–140
    [Google Scholar]
  4. 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
    [Google Scholar]
  5. Büchler M., Tisljar U., Wolf D. H. 1994; Proteinase yscD (oligopeptidase yscD) structure, function and relationship of the yeast enzyme with mammalian thimet oligopeptidase (metallo-endopeptidase, EP 24.15). Eur J Biochem 219:627–639
    [Google Scholar]
  6. Camargo A. C. M., Caldo H., Reis M. L. 1979; Susceptibility of a peptide derived from bradykinin to hydrolysis by brain endo-oligopeptidases and pancreatic proteinases. J Biol Chem 254:5304–5307
    [Google Scholar]
  7. Checler F., Vincent J.-P., Kitabgi P. 1986; Purification and characterization of a novel neurotensin-degrading peptidase from rat brain synaptic membranes. J Biol Chem 261:11274–11281
    [Google Scholar]
  8. Cohen J. 1991 Clinical manifestations and management of aspergillosis in the compromised patients. . In Fungal Infection in the Compromised Patient , 2nd edn, pp. 117–152 . Edited by Warnoclc D. W., Richardson M. D. New York: John Wiley;
    [Google Scholar]
  9. Conlin C. A., Miller C. G. 1992; Cloning and nucleotide sequence of opdA, the gene encoding oligopeptidase A in Salmonella typhimurium . J Bacteriol 174:1631–1640
    [Google Scholar]
  10. Conlin C. A., Trun N. J., Silhavy T. J., Miller C. G. 1992; Escherichia coli prlC encodes an endopeptidase and is homologous to the Salmonella typhimurium opdA gene. J Bacteriol 174:5881–5887
    [Google Scholar]
  11. Devereux J., Haeberli P., Smithies O. 1984; A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12:387–395
    [Google Scholar]
  12. Dioszegi M., Cannon P., Van Wart H. E. 1995; Vertebrate collagenases. Methods Enzymol 248:413–431
    [Google Scholar]
  13. Frischauf A. M., , Lehrach H., Poustka A., Murray N. 1983; Lambda replacement vectors carrying polylinker sequences. J Mol Biol 170:827–842
    [Google Scholar]
  14. Girardin H., Latgé, J.-P., Skirantha T., Morrow B., Soil D. 1993; Development of DNA probes for fingerprinting Aspergillus fumigatus . J Clin Microbiol 31:1547–1554
    [Google Scholar]
  15. Hanahan D., Jessee J., Bloom F. R. 1991; Plasmid transformation of Escherichia coli and other bacteria. Methods Enzymol 204:63–113
    [Google Scholar]
  16. Henrich B., Becker S., Schroeder U., Plapp R. 1993; dcp gene of Escherichia coli: cloning, sequencing, transcript mapping, and characterization of the gene product. J Bacteriol 175:7290–7300
    [Google Scholar]
  17. Ibrahim-Granet O., Bertrand O., Debeaupuis J.-P., Planchenault T., Diaquin M., Dupont B. 1994; Aspergillus fumigatus metalloproteinase that hydrolyses native collagen: purification by dye-binding chromatography. Protein Expr Purif 5:84–88
    [Google Scholar]
  18. Ibrahim-Granet O., Hernandez F. H., Chevrier G., Dupont B. 1996; Expression of PZ-peptidases by cultures of several pathogenic fungi. Purification and characterization of a colla genase from Trychophyton schoenleinii . J Med Vet Mycol 34:83–90
    [Google Scholar]
  19. Isaya G., Kalousek F., Rosenberg L. E. 1992; Sequence analysis of rat mitochondrial intermediate peptidase: similarity to zinc metallopeptidases and to a putative yeast homologue. Proc Natl Acad Sci USA 89:8317–8321
    [Google Scholar]
  20. Isaya G., Miklos D., Rollins R. A. 1994; MIP1, a new yeast gene homologous to the rat mitochondrial intermediate peptidase gene, is required for oxidative metabolism in Saccharomyces cerevisiae . Mol Cell Biol 14:5603–5616
    [Google Scholar]
  21. Jaton-Ogay K., Suter M., Crameri R., Faichetto R., Fatih A., Monod M. 1992; Nucleotide sequence of a genomic and a cDNA clone encoding an extracellular alkaline protease of Aspergillus fumigatus . FEMS Microbiol Lett 92:163–168
    [Google Scholar]
  22. Jaton-Ogay K., Paris S., Huerre M., Quadroni M., Faichetto R., Togni G., Latgé, J.-P. & Monod M. 1994; Cloning and disruption of the gene encoding an extracellular metalloprotease of Aspergillus fumigatus . Mol Microbiol 14:917–928
    [Google Scholar]
  23. Jiang W., Bond J. S. 1992; Families of metalloendopeptidases and their relationships. FEBS Lett 312:110–114
    [Google Scholar]
  24. Kato A., Sugiura N., Hagiwara H., Hirose S. 1994; Cloning, amino acid sequence and tissue distribution of porcine thimet oligopeptidase. A comparison with soluble angiotensin-binding protein. Eur J Biochem 221:159–165
    [Google Scholar]
  25. Kawabata S., Nakagawa K., Muta T., Iwanaga S., Davie E. W. 1993; Rabbit liver microsomal endopeptidase with substrate specificity for processing proproteins is structurally related to rat testes metalloendopeptidase 24.15. J Biol Chem 268:12498–12503
    [Google Scholar]
  26. Kawasaki H., Emori Y., Suzuki K. 1990; Production and separation of peptides from proteins stained with Coomassie brilliant blue R-250 after separation by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Anal Biochem 191:332–336
    [Google Scholar]
  27. Maeda H., Morihara K. 1995; Serralysin and related bacterial proteinases. Methods Enzymol 248:395–413
    [Google Scholar]
  28. Matthews B. W., Jansonius J. N., Colman P. M., Schoenborn P., Duporque D. 1972; Three-dimensional structure of thermolysin. Nat New Biol 238:37–41
    [Google Scholar]
  29. Monod M., Paris S., Sarfati J., Jaton-Ogay K., Ave P., Latgé J.-P. 1993; Virulence of alkaline protease-deficient mutants of Aspergillus fumigatus . FEMS Microbiol Lett 106:39–46
    [Google Scholar]
  30. Orlowski M., Michaud C., Chu G. 1983; A soluble metallo-endopeptidase from rat brain. Purification of the enzyme and determination of specificity with synthetic and natural peptides. Eur J Biochem 135:81–88
    [Google Scholar]
  31. Pierotti A., Dong K., W” Glucksman M. J., Orlowski M., Roberts J. L. 1990; Molecular cloning and primary structure of rat testes metalloendopeptidase. Biochemistry 29:10323–10329
    [Google Scholar]
  32. Ramesh M. V., Sirakova T. D., Kolattukudy P. E. 1995; Cloning and characterization of the cDNAs and genes (mep20) encoding homologous metalloproteinases from Aspergillus flavus and Aspergillus fumigatus . Gene 165:121–125
    [Google Scholar]
  33. Rawlings N. D., Barrett A. J. 1995; Evolutionary families of metallopeptidases. Methods Enzymol 248:183–228
    [Google Scholar]
  34. Sambrook J., Fritsch E. F., Maniatis T. 1989 Molecular Cloning: a Laboratory Manual , 2nd edn Cold Spring Harbor; NY: Cold Spring Harbor Laboratory:
    [Google Scholar]
  35. Sanger F., Nicklen S., Coulson R. A. 1977; DNA sequencing with chain terminating inhibitors. Proc Natl Acad Sci USA 74:5463–5467
    [Google Scholar]
  36. Serizawa A., Dando P. M., Barrett A. J. 1995; Characterization of a mitochondrial metallopeptidase reveals neurolysin as a homologue of thimet oligopeptidase. J Biol Chem 270:2092–2098
    [Google Scholar]
  37. Smith J. M., Tang C. M., Noorden S. V., Holden D. W. 1994; Virulence of Aspergillus fumigatus double mutants lacking restrictocin and an alkaline protease in a low-dose model of invasive pulmonary aspergillosis. Infect Immun 62:5247–5254
    [Google Scholar]
  38. Stynen D., Sarfati J., Goris A., Prgvost M.-C., Lesourd M., Kamphuis H., Darras V., Latgé J.-P. 1992; Rat monoclonal antibodies against Aspergillus galactomannan. Infect Immun 60:2237–2245
    [Google Scholar]
  39. Tang C. M., Cohen J., Krausz T., van Noorden S., Holden D. W. 1993; The alkaline protease of Aspergillus fumigatus is not a virulence determinant in two murine models of invasive pulmonary aspergillosis. Infect Immun 61:1650–1656
    [Google Scholar]
  40. Thompson A., Huber G., Malherbe P. 1995; Cloning and functional expression of a metalloendopeptidase from human brain with the ability to cleave a beta-APP substrate peptide. Biochem Biophys Res Commun 213:66–73
    [Google Scholar]
  41. Wünsch E., Heidrich H. G. 1963; Darstellung von prolinpeptiden. III. Ein neues substrat zur bestimmung der kollagenase. Hoppe-Seyler’s Z Physiol Chem 332:300–304
    [Google Scholar]
  42. Yanisch-Perron C., Vieira J., Messing J. 1985; Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectors. Gene 33:103–119
    [Google Scholar]
/content/journal/micro/10.1099/00221287-143-7-2247
Loading
/content/journal/micro/10.1099/00221287-143-7-2247
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error