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Journal of Bacteriology, February 1999, p. 923-933, Vol. 181, No. 3
Department of Microbiology,
Received 30 June 1998/Accepted 16 November 1998
Clostridium histolyticum collagenase contains a number
of different active components. Previously we have shown that
colH encodes a 116-kDa collagenase (ColH) and a 98-kDa
gelatinase. We purified a different 116-kDa collagenase (ColG)
from the culture supernatant and sequenced its gene (colG).
We also identified four other gelatinases (105, 82, 78, and 67 kDa) and
determined their N-terminal amino acid sequences, all of which
coincided with that of either ColG or ColH. Hybridization experiments
showed that each gene is present in a single copy and each gene is
transcribed into a single mRNA. These results suggest that all the
gelatinases are produced from the respective full-length collagenase by
the proteolytic removal of C-terminal fragments. The substrate
specificities of the enzymes suggest that colG and
colH encode class I and class II enzymes,
respectively. Analysis of their DNA locations by pulsed-field gel
electrophoresis and nucleotide sequencing of their surrounding regions
revealed that the two genes are located in different sites on the
chromosome. C. histolyticum colG is more similar to
C. perfringens colA than to colH in terms
of domain structure. Both colG and colA have a
homologous gene, mscL, at their 3' ends. These results
suggest that gene duplication and segment duplication have occurred in
an ancestor cell common to C. histolyticum and C. perfringens and that further divergence of the
parent gene produced colG and colA.
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Gene Duplication and Multiplicity of
Collagenases in Clostridium histolyticum
*
Corresponding author. Mailing address: Department of
Microbiology, Faculty of Medicine, Kagawa Medical University,
1750-1 Ikenobe, Miki-cho, Kagawa 761-0793, Japan. Phone: 81 (87)
891-2129. Fax: 81 (87) 898-7109. E-mail:
microbio{at}kms.ac.jp.
Journal of Bacteriology, February 1999, p. 923-933, Vol. 181, No. 3
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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