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Journal of Bacteriology, March 2007, p. 1627-1632, Vol. 189, No. 5
0021-9193/07/$08.00+0 doi:10.1128/JB.01714-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Department of Microbiology and Immunology, University of Miami Miller School of Medicine, Miami, Florida
Received 6 November 2006/ Accepted 14 December 2006
The expression of the inner membrane protein NlpA is repressed by the enterotoxigenic Escherichia coli (ETEC) virulence regulator Rns, a member of the AraC/XylS family. The Rns homologs CfaD from ETEC and AggR from enteroaggregative E. coli also repress expression of nlpA. In vitro DNase I and potassium permanganate footprinting revealed that Rns binds to a site overlapping the start codon of nlpA, preventing RNA polymerase from forming an open complex at nlpAp. A second Rns binding site between positions 152 and 195 relative to the nlpA transcription start site is not required for repression. NlpA is not essential for growth of E. coli under laboratory conditions, but it does contribute to the biogenesis of outer membrane vesicles. As outer membrane vesicles have been shown to contain ETEC heat-labile toxin, the repression of nlpA may be an indirect mechanism through which the virulence regulators Rns and CfaD limit the release of toxin.
Published ahead of print on 22 December 2006.
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