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J. Bacteriol., May 1996, 2986-2988, Vol 178, No. 10
M Mondigler and M Ehrmann
A seven-amino-acid cleavage site specific for tobacco etch virus (TEV)
protease was introduced into SecA at two separate positions after amino
acids 195 and 252. Chromosomal wild-type secA was replaced by these secA
constructs. Simultaneous expression of TEV protease led to cleavage of both
SecA derivatives. In the functional SecA dimer, proteolysis directly
indicated surface exposure of the TEV protease cleavage sites. Cleavage of
SecA near residue 195 generated an unstable proteolysis product and a
secretion defect, suggesting that this approach could be used to inactivate
essential proteins in vivo.
Copyright © 1996, American Society for Microbiology
Site-specific proteolysis of the Escherichia coli SecA protein in vivo
Fakultat fur Biologie, Universitat Konstanz, Germany.
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