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Science 15 September 1989:
Vol. 245. no. 4923, pp. 1246 - 1249
DOI: 10.1126/science.2476847
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Articles

Science, Vol 245, Issue 4923, 1246-1249
Copyright © 1989 by American Association for the Advancement of Science

articles

Activation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate

R Utsumi, RE Brissette, A Rampersaud, SA Forst, K Oosawa, and M Inouye

Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway 08854.

The Tar chemoreceptor of Escherichia coli is a membrane-bound sensory protein that facilitates bacterial chemotaxis in response to aspartate. The EnvZ molecule has a membrane topology similar to Tar and is a putative osmosensor that is required for osmoregulation of the genes for the major outer membrane porin proteins, OmpF and OmpC. The cytoplasmic signaling domain of Tar was replaced with the carboxyl portion of EnvZ, and the resulting chimeric receptor activated transcription of the ompC gene in response to aspartate. The activation of ompC by the chimeric receptor was absolutely dependent on OmpR, a transcriptional activator for ompF and ompC.


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