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Journal of Bacteriology, October 1998, p. 5458-5462, Vol. 180, No. 20
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Efficiency of the pTF-FC2 pas Poison-Antidote Stability System in Escherichia coli Is Affected by the Host Strain, and Antidote Degradation Requires the Lon Protease

Anthony S. G. Smith and Douglas E. Rawlings*

Department of Microbiology, University of Cape Town, Rondebosch 7700, South Africa

Received 13 February 1998/Accepted 22 June 1998

The stabilization of a test plasmid by the proteic, poison-antidote plasmid addiction system (pas) of plasmid pTF-FC2 was host strain dependent, with a 100-fold increase in stability in Escherichia coli CSH50, a 2.5-fold increase in E. coli JM105, and no detectable stabilization in E. coli strains JM107 and JM109. The lethality of the PasB toxin was far higher in the E. coli strains in which the pas was most effective. Models for the way in which poison-antidote systems stabilize plasmids require that the antidote have a much higher rate of turnover than that of the toxin. A decrease in host cell death following plasmid loss from an E. coli lon mutant and a decrease in plasmid stability suggested that the Lon protease plays a role in the rate of turnover of PasA antidote.

* Corresponding author. Present address: Department of Microbiology, University of Stellenbosch, Stellenbosch 7600, South Africa. Phone: 27 21 808 4866. Fax: 27 21 808 3611. E-mail: der{at}maties.sun.ac.za.

Journal of Bacteriology, October 1998, p. 5458-5462, Vol. 180, No. 20
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

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  • Gerdes, K. (2000). Toxin-Antitoxin Modules May Regulate Synthesis of Macromolecules during Nutritional Stress. J. Bacteriol. 182: 561-572 [Full Text]  


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