The periplasmic protein MppA requires an additional mutated locus to repress marA expression in Escherichia coli.
نویسندگان
چکیده
Escherichia coli strain TP985, which has an insertional mutation in the gene for the periplasmic murein tripeptide binding protein MppA, was previously reported to overproduce MarA and exhibit a multiple-antibiotic resistance (Mar) phenotype (H. Li and J. T. Park, J. Bacteriol. 181:4842-4847, 1999). We found that TP985 contained a previously unrecognized marR mutation which was responsible for the Mar phenotype. Transduction of the mppA mutation from TP985 to another wild-type strain did not affect antibiotic susceptibility. Overproduction of MppA repressed marA transcription in TP985 but not in other mppA or marR mutants. Therefore, TP985 contains an additional unknown mutation(s) that facilitates the repression of marA expression by MppA.
منابع مشابه
The periplasmic protein MppA is not involved in regulation of marA in Escherichia coli.
The marRAB operon of Escherichia coli is self-repressed by MarR, while the MarA protein activates a number of promoters, including those for the AcrAB/TolC multidrug efflux pump (1, 4, 5). Inactivation of marR leads to a “Mar” multipleantibiotic resistance phenotype. In 1999, the mppA gene was reported to be a novel factor involved in the regulation of the marRAB operon (3). Strain TP985 had be...
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ورودعنوان ژورنال:
- Journal of bacteriology
دوره 185 4 شماره
صفحات -
تاریخ انتشار 2003