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Journal of Bacteriology, November 2002, p. 6109-6114, Vol. 184, No. 22
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.22.6109-6114.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

The PrpC Serine-Threonine Phosphatase and PrkC Kinase Have Opposing Physiological Roles in Stationary-Phase Bacillus subtilis Cells

Tatiana A. Gaidenko, Tae-Jong Kim, and Chester W. Price*

Department of Food Science and Technology, University of California, Davis, California 95616

Received 18 December 2001/ Accepted 19 August 2002

Loss of the PrpC serine-threonine phosphatase and the associated PrkC kinase of Bacillus subtilis were shown to have opposite effects on stationary-phase physiology by differentially affecting cell density, cell viability, and accumulation of ß-galactosidase from a general stress reporter fusion. These pleiotropic effects suggest that PrpC and PrkC have important regulatory roles in stationary-phase cells. Elongation factor G (EF-G) was identified as one possible target of the PrpC and PrkC pair in vivo, and purified PrpC and PrkC manifested the predicted phosphatase and kinase activities against EF-G in vitro.

* Corresponding author. Mailing address: Department of Food Science and Technology, University of California, Davis, CA 95616. Phone: (530) 752-1596. Fax: (530) 752-4759. E-mail: cwprice{at}ucdavis.edu.

Journal of Bacteriology, November 2002, p. 6109-6114, Vol. 184, No. 22
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.22.6109-6114.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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