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Journal of Bacteriology, February 2003, p. 1465-1469, Vol. 185, No. 4
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.4.1465-1469.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

The Periplasmic Protein MppA Requires an Additional Mutated Locus To Repress marA Expression in Escherichia coli

Xiaowen Bina,^1,2 Vincent Perreten,^1,2, and Stuart B. Levy^1,2,3*

Center for Adaptation Genetics and Drug Resistance,¹ Departments of Molecular Biology and Microbiology ,² of Medicine, Tufts University School of Medicine, Boston, Massachusetts 02111³

Received 14 August 2002/ Accepted 20 November 2002

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.

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* Corresponding author. Mailing address: Center for Adaptation Genetics and Drug Resistance, Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111. Phone: (617) 636-6764. Fax: (617) 636-0458. Email: stuart.levy{at}tufts.edu.

Present address: Institute for Veterinary Bacteriology, University of Berne, CH-3012 Bern, Switzerland.

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Journal of Bacteriology, February 2003, p. 1465-1469, Vol. 185, No. 4
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.4.1465-1469.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

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