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Applied and Environmental Microbiology, February 2000, p. 476-480, Vol. 66, No. 2
Department of Biological Sciences, Korea
Advanced Institute of Science and Technology,1
and Research Center for New Bio-Materials in
Agriculture,2 Taejon, 305-701, Republic of Korea
Received 7 July 1999/Accepted 3 November 1999
Staphylokinase (SAK), a polypeptide secreted by
Staphylococcus aureus, is a plasminogen activator with a
therapeutic potential in thrombosis diseases. A Bacillus
subtilis strain which is multiply deficient in exoproteases was
transformed by an expression plasmid carrying a promoter and a signal
sequence of subtilisin fused in frame with the sak open
reading frame. However, the amount of SAK secretion was marginal (45 mg/liter). In contrast, disruption of the wprA gene, which
encodes a subtilisin-type protease, strongly promoted the production of
SAK in the stationary phase (181 mg/liter). In addition, the
extracellular stability of mature SAK was dramatically enhanced. These
data indicate a significant role of the wprA gene product
in degrading foreign proteins, both during secretion and in the
extracellular milieu.
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Enhancement of Secretion and Extracellular
Stability of Staphylokinase in Bacillus subtilis by
wprA Gene Disruption
*
Corresponding author. Mailing address: Department of
Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), Taejon 305-701, Korea. Phone: 82-42-869-2631. Fax:
82-42-869-2610. E-mail: jhchung{at}sorak.kaist.ac.kr.
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