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(Received for publication, September 24, 1996)
From the Department of Bacterial Infections, Research Institute for
Microbial Diseases, Osaka University, Yamadaoka 3-1, Suita,
Osaka 565, Japan
Vibrio cholerae synthesizes a toxin
named El Tor cytolysin/hemolysin, which lyses erythrocytes and other
mammalian cells. This toxin is encoded by the hlyA gene and
is synthesized as a precursor form, prepro-HlyA. Prepro-HlyA consists
of, from the amino terminus of this protein, a signal peptide, a
pro-region, and a mature region. The pro-region is cleaved off
extracellularly resulting in activation. To analyze the role of the
pro-region, we substituted the native hlyA gene with the
pro-region-deleted hlyA gene
(hlyA
Volume 272, Number 2,
Issue of January 10, 1997
pp. 1338-1343
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
pro). The hemolytic activity of the
mutant organism was markedly decreased; the product of the
hlyApro gene, secreted in the periplasm, was
degraded. To compare their abilities to form tertiary structure, the
purified mature- and pro-HlyA were denatured and then renatured by
reducing the concentration of denaturant; the denatured pro-HlyA
recovered almost all activity while the mature-HlyA was not renatured.
The sequences of the pro-region and a molecular chaperone, Hsp90, were
similar. The pro-region expressed in Escherichia coli
containing the hlyApro gene increased the
cytolytic activity. The purified pro-region peptide also facilitated
renaturation of the denatured mature HlyA. These results suggest that
the pro-region possibly guides the folding of the cytolysin similar to
a molecular chaperone; the pro-region and molecular chaperones share
common function and structure.
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