Gene duplication and multiplicity of collagenases in Clostridium histolyticum

Journal of Bacteriology

Volumn 181, Issue 3, 1999, Pages 923-933

  Matsushita, Osamu ^a   Jung, Chang Min ^a   Katayama, Seiichi ^a   Minami, Junzaburo ^a   Takahashi, Yukie ^b   Okabe, Akinobu ^a  

^a KAGAWA UNIVERSITY   (Japan)

^b FUKUYAMA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGENASE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CLOSTRIDIUM HISTOLYTICUM; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME SPECIFICITY; GENE DUPLICATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL;

CLOSTRIDIUM HISTOLYTICUM; CLOSTRIDIUM PERFRINGENS; COLA; PROKARYOTA;

EID: 0032891451     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.3.923-933.1999     Document Type: Article

References (49)

1. Aiba, H., S. Adhya, and B. de Crombrugghe. 1981. Evidence for two functional, gal promoters in intact Escherichia coli cells. J. Biol. Chem. 256:11905-11910.
2. Altschul, S. F., W. Gish, W. Miller, E. W. Myers, and D. J. Lipman. 1990. Basic local alignment search tool. J. Mol. Biol. 215:403-410.
3. Becker, A., F. Theuring, M. Gottwald, K. Kauser, W.-D. Schleuning, and P. Donner. 1994. Purification of human big endothelin I derived through cleavage with collagenase and dipeptidylpeptidase IV from a fusion protein expressed in Escherichia coli. Protein Expr. Purif. 5:50-56.
4. Bethesda Research Laboratories. 1986. BRL pUC host: E. coli DH5α™ competent cells. Focus 8:9.
5. Birkedal-Hansen, H., and R. E. Taylor. 1982. Detergent-activation of latent collagenase and resolution of its component molecules. Biochem. Biophys. Res. Commun. 107:1173-1178.
6. Bond, M. D., and H. E. Van Wart. 1984. Characterization of the individual collagenases from Clostridium histolyticum. Biochemistry 23:3085-3091.
7. Bond, M. D., and H. E. Van Wart. 1984. Relationship between the individual collagenases of Clostridium histolyticum: evidence for evolution by gene duplication. Biochemistry 23:3092-3099.
8. Brynestad, S., B. Synstad, and P. E. Granum. 1997. The Clostridium perfringens enterotoxin gene is on a transposable element in type A human food poisoning strains. Microbiology 143:2109-2115.
9. Canard, B., and S. T. Cole. 1989. Genome organization of the anaerobic pathogen Clostridium perfringens. Proc. Natl. Acad. Sci. USA 86:6676-6680.
10. Cornillot, E., B. Saint-Joanis, G. Daube, S. Katayama, P. E. Granum, B. Canard, and S. T. Cole. 1995. The enterotoxin gene (cpe) of Clostridium perfringens can be chromosomal or plasmid-borne. Mol. Microbiol. 15:639-647.
11. de Bruijn, F. J., J. R. Lupski, and G. M. Weinstock. 1998. Bacterial genomes: physical structure and analysis. Chapman & Hall, New York, N.Y.
12. Fukunaga, M., Y. Yanagihara, and M. Sohnaka. 1992. The 23S/5S ribosomal RNA genes (rrl/rrf) are separate from the 16S ribosomal RNA gene (rrs) in Borrelia burgdorferi, the aetiological agent of Lyme disease. J. Gen. Microbiol. 138:871-877.
13. Garnier, T., B. Canard, and S. T. Cole. 1991. Cloning, mapping, and molecular characterization of the rRNA operons of Clostridium perfringens. J. Bacteriol. 173:5431-5438.
14. Gelbard, M. K., K. James, P. Riach, and F. Dorey, 1993. Collagenase versus placebo in the treatment of Peyronie's disease: a double-blind study. J. Urol. 149:56-58.
15. Hanada, K., I. Yamato, and Y. Anraku. 1988. Purification and reconstitution of Escherichia coli proline carrier using a site specifically cleavable fusion protein. J. Biol. Chem. 263:7181-7185.
16. Inoue, K., and H. Iida. 1970. Conversion of toxigenicity in Clostridium botulinum type C. Jpn. J. Microbiol. 14:87-89.
17. Inoue, K., and H. Iida. 1971. Phage-conversion of toxigenicity in Clostridium botulinum types C and D. Jpn. J. Med. Sci. Biol. 24:53-56.
18. The International Polycystic Kidney Disease Consortium. 1995. Polycystic kidney disease: the complete structure of the PKD1 gene and its protein. Cell 81:289-298.
19. Jung, C.-M., O. Matsushita, S. Katayama, J. Minami, I. Ohhira, and A. Okabe. 1996. Expression of the colH gene encoding Clostridium histolyticum collagenase in Bacillus subtilis and its application to enzyme purification. Microbiol. Immunol. 40:923-929.
20. Jung, C.-M., O. Matsushita, S. Katayama, J. Minami, J. Sakurai, and A. Okabe. Analysis of the catalytic center in the Clostridium histolyticum ColH collagenase. Submitted for publication.
21. Katayama, S., B. Dupuy, G. Daube, B. China, and S. T. Cole. 1996. Genome mapping of Clostridium perfringens strains with I-Ceul shows many virulence genes to be plasmid-borne. Mol. Gen. Genet. 251:720-726.
22. Katayama, S.-I., B. Dupuy, T. Garnier, and S. T. Cole. 1995. Rapid expansion of the physical and genetic map of the chromosome of Clostridium perfringens CPN50. J. Bacteriol. 177:5680-5685.
23. Kono, T. 1968. Purification and partial characterization of collagenolytic enzymes from Clostridium histolyticum. Biochemistry 7:1106-1114.
24. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
25. Lanzillo, J. J. 1991. Chemiluminescent nucleic acid detection with digoxigenin-labeled probes: a model system with probes for angiotensin converting enzyme which detect less than one attomole of target DNA. Anal. Biochem. 194:45-53.
26. Lwebuga-Mukasa, J. S., E. Harper, and P. Taylor. 1976. Collagenase enzymes from Clostridium: characterization of individual enzymes. Biochemistry 15:4736-4741.
27. Mandl, I., S. Keller, and J. Manahan. 1964. Multiplicity of Clostridium histolyticum collagenase. Biochemistry 3:1737-1741.
28. Maniatis, T., E. F. Fritsch, and J. Sambrook. 1982. Molecular cloning: a laboratory manual. Cold Spring Harbor laboratory. Cold Spring Harbor, N.Y.
29. Matsushita, O., C.-M. Jung, J. Minami, S. Katayama, N. Nishi, and A. Okabe. 1998. A study of the collagen-binding domain of a 116-kDa Clostridium histolyticum collagenase. J. Biol. Chem. 273:3643-3648.
30. Matsushita, O., C. M. Jung, and A. Okabe. 1995. Identification of the gene encoding a mechanosensitive channel MscL, homologue in Clostridium perfringens. Gene 165:147-148.
31. Matsushita, O., K. Yoshihara, S.-I. Katayama, J. Minami, and A. Okabe. 1994. Purification and characterization of a Clostridium perfringens 120-kilo-dalton collagenase and nucleotide sequence of the corresponding gene. J. Bacteriol. 176:149-156.
32. Messing, J. 1983. New M13 vectors for cloning. Methods Enzymol. 101:20-78.
33. Miyoshi, M., and J. Rosenbloom. 1974. General proteolytic activity of highly purified preparations of clostridial collagenase. Connect. Tissue Res. 2:77-84.
34. Mookhtiar, K. A., and H. E. Van Wart. 1992. Clostridium histolyticum collagenases: a new look at some old enzymes. Matrix Suppl. 1:116-126.
35. Nielsen, H., J. Engelbrecht, S. Brunak, and G. von Heijne. 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1-6.
36. Nishi, N., O. Matsushita, K. Yuube, H. Miyanaka, A. Okabe, and F. Wada. 1998. Collagen-binding growth factors: production and characterization of functional fusion proteins having a collagen-binding domain. Proc. Natl. Acad. Sci. USA 95:7018-7023.
37. Pearson, W. R., and D. J. Lipman. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85:2444-2448.
38. Peterkofsky, B. 1982. Bacterial collagenase. Methods Enzymol. 82:453-471.
39. Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463-5467.
40. Seglen, P. O. 1976. Preparation of isolated rat liver cells. Methods Cell Biol. 13:29-83.
41. Starkweather, K. D., S. Lattuga, L. C. Hurst, M. A. Badalamente, F. Guilak, S. P. Sampson, A. Dowd, and D. Wisch. 1996. Collagenase in the treatment of Dupuytren's disease: an in vitro study. J. Hand Surg. 21:490-495.
42. Takeuchi, H., Y. Shibano, K. Morihara, J. Fukushima, S. Inami, B. Keil, A.-M. Gilles, S. Kawamoto, and K. Okuda. 1992. Structural gene and complete amino acid sequence of Vibrio alginolyticus collagenase. Biochem. J. 281:703-7118.
43. Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
44. Warren, G. H., and J. Gray. 1961. A simplified culture medium for the production of collagenase. Nature (London) 192:755-756.
45. Wilson, M. J., M. Strasser, M. M. Vogel, and A. A. Sinha. 1991. Calcium-dependent and calcium-independent gelatinolytic proteinase activities of the rat ventral prostate and its secretion: characterization and effect of castration and testosterone treatment. Biol. Reprod. 44:776-785.
46. Wolters, G. H. J., G. H. Vos-Scheperkeuter, H.-C. Lin, and R. Van Schilfgaarde. 1995. Different roles of class I and class II Clostridium histolyticum collagenase in rat pancreatic islet isolation. Diabetes 44:227-233.
47. Wünsch, E., and H.-G. Heidrich. 1963. Zur quantitativen Bestimmung der Kollagenase. Hoppe-Seyler's Z. Physiol. Chem. 333:149-151.
48. Yoshida, E., and H. Noda. 1965. Isolation and characterization of collagenases I and II from Clostridium histolyticum. Biochim. Biophys. Acta 105: 562-574.
49. Yoshihara, K., O. Matsushita, J. Minami, and A. Okabe. 1994. Cloning and nucleotide sequence analysis of the colH gene from Clostridium histolyticum encoding a collagenase and a gelatinase. J. Bacteriol. 176:6489-6496.