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J. Biol. Chem., Vol. 280, Issue 15, 14765-14772, April 15, 2005
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Transcriptional Regulation of the 4-Amino-4-deoxy-L-arabinose Biosynthetic Genes in Yersinia pestis*
From the Department of Molecular Microbiology, Howard Hughes Medical Institute, Washington University School of Medicine, St. Louis, Missouri 63110
Inducible membrane remodeling is an adaptive mechanism that enables Gram-negative bacteria to resist killing by cationic antimicrobial peptides and to avoid eliciting an immune response. Addition of 4-amino-4-deoxy-L -arabinose (4-aminoarabinose) moieties to the phosphate residues of the lipid A portion of the lipopolysaccharide decreases the net negative charge of the bacterial membrane resulting in protection from the cationic antimicrobial peptide polymyxin B. In Salmonella enterica serovar Typhimurium, the PmrA/PmrB two-component regulatory system governs resistance to polymyxin B by controlling transcription of the 4-aminoarabinose biosynthetic genes. Transcription of PmrA-activated genes is induced by Fe3+, which is sensed by PmrA cognate sensor PmrB, and by low Mg2+, in a mechanism that requires not only the PmrA and PmrB proteins but also the Mg2+-responding PhoP/PhoQ system and the PhoP-activated PmrD protein, a post-translational activator of the PmrA protein. Surprisingly, Yersinia pestis can promote PhoP-dependent modification of its lipid A with 4-aminoarabinose despite lacking a PmrD protein. Here we report that Yersinia uses different promoters to transcribe the 4-aminoarabinose biosynthetic genes pbgP and ugd depending on the inducing signal. This is accomplished by the presence of distinct binding sites for the PmrA and PhoP proteins in the promoters of the pbgP and ugd genes. Our results demonstrate that closely related bacterial species may use disparate regulatory pathways to control genes encoding conserved proteins.
Received for publication, December 9, 2004 , and in revised form, January 28, 2005.
* This work was supported by grants from the National Institutes of Health (to E. A. G). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
An Investigator of the Howard Hughes Medical Institute. To whom correspondence should be addressed: Dept. of Molecular Microbiology, Howard Hughes Medical Institute, WA University School of Medicine, 660 S. Euclid Ave., Campus Box 8230, St. Louis, MO 63110. Tel.: 314-362-3692; Fax: 314-747-8228; E-mail: groisman{at}borcim.wustl.edu.
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