EFFICIENCY OF THE PTF-FC2 PAS POISON-ANTIDOTE STABILITY SYSTEM IN ESCHERICHIA-COLI IS AFFECTED BY THE HOST STRAIN, AND ANTIDOTE DEGRADATIONREQUIRES THE LON PROTEASE
Asg. Smith et De. Rawlings, EFFICIENCY OF THE PTF-FC2 PAS POISON-ANTIDOTE STABILITY SYSTEM IN ESCHERICHIA-COLI IS AFFECTED BY THE HOST STRAIN, AND ANTIDOTE DEGRADATIONREQUIRES THE LON PROTEASE, Journal of bacteriology (Print), 180(20), 1998, pp. 5458-5462
The stabilization of a test plasmid by the proteic, poison-antidote pl
asmid addiction system (pas) of plasmid pTF-FC2 was host strain depend
ent, with a 100-fold increase in stability in Escherichia call CSH50,
a 2.5-fold increase in E. coli JM105, and no detectable stabilization
in E. call strains JM107 and JM109. The lethality of the PasB toxin wa
s far higher in the E. coli strains in which the pas was most effectiv
e. Models for the way in which poison-antidote systems stabilize plasm
ids require that the antidote have a much higher rate of turnover than
that of the toxin. A decrease in host cell death following plasmid lo
ss from an E. call ion mutant and a decrease in plasmid stability sugg
ested that the Lon protease plays a role in the rate of turnover of Pa
sA antidote.