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Journal of Bacteriology, December 1999, p. 7185-7191, Vol. 181, No. 23
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Providencia stuartii Genes Activated by Cell-to-Cell Signaling and Identification of a Gene Required for Production or Activity of an Extracellular Factor

Philip N. Rather,1,2,* Xuedong Ding,1 Rita R. Baca-DeLancey,1 and Soofia Siddiqui2

Departments of Medicine and Molecular Biology and Microbiology, Case Western Reserve University School of Medicine,1 and Research Service, Veterans Affairs Medical Center,2 Cleveland, Ohio 44106

Received 25 August 1999/Accepted 15 September 1999

By utilizing reporter transposons, five Providencia stuartii genes that are activated by the accumulation of self-produced extracellular signals have been identified. These genes have been designated cma for conditioned medium activated. The presence of conditioned medium from stationary-phase cultures grown in rich media resulted in the premature activation of each gene in cells at early log phase, with activation values ranging from 6- to 26-fold. Preparation of conditioned medium from an M9 salts medium and fractionation by gel filtration chromatography resulted in fractions within the included volume which activated three of the cma fusions. In addition, depending on the reporter fusion, peak activity was found in different fractions. The partially purified factors activated in a dose-dependent manner. Characterization of the factors activating the cma fusions indicated that they were stable to heat, alkali, and acid. Furthermore, for each cma fusion, factor activity was not reproduced by the addition of homoserine lactone, homocysteine thiolactone, pyruvate, Casamino Acids, or alpha -ketoglutarate. The identities of three cma genes have been determined and revealed physiological roles in amino acid biosynthesis and nutrient import. To begin to address the pathways for production of or response to the extracellular factors, we have identified a locus, aarA, that is required for the activation of four cma fusions. The AarA product was required for factor activity in extracellular supernatants, indicating a possible role in biosynthesis or export.

* Corresponding author. Mailing address: Division of Infectious Diseases, BRB-10, Case Western Reserve University School of Medicine, 10900 Euclid Ave., Cleveland, OH 44106. Phone: (216) 368-0733. Fax: (216) 368-2034. E-mail: pxr17{at}po.cwru.edu.

Journal of Bacteriology, December 1999, p. 7185-7191, Vol. 181, No. 23
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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