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Journal of Bacteriology, April 2007, p. 2637-2645, Vol. 189, No. 7
0021-9193/07/$08.00+0     doi:10.1128/JB.01798-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Negative Regulation of Bacillus anthracis Sporulation by the Spo0E Family of Phosphatases ^,

The Scripps Research Institute, Department of Molecular and Experimental Medicine, Division of Cellular Biology, 10550 North Torrey Pines Road, La Jolla, California 92037

Received 28 November 2006/ Accepted 18 January 2007

The initiation of sporulation in Bacillus species is controlled by the phosphorelay signal transduction system. Multiple regulatory elements act on the phosphorelay to modulate the level of protein phosphorylation in response to cellular, environmental, and metabolic signals. In Bacillus anthracis nine possible histidine sensor kinases can positively activate the system, while two response regulator aspartyl phosphate phosphatases of the Rap family negatively impact the pathway by dephosphorylating the Spo0F intermediate response regulator. In this study, we have characterized the B. anthracis members of the Spo0E family of phosphatases that specifically dephosphorylate the Spo0A response regulator of the phosphorelay and master regulator of sporulation. The products of four genes were able to promote the dephosphorylation of Spo0AP in vitro. The overexpression of two of these B. anthracis Spo0E-like proteins from a multicopy vector consistently resulted in a sporulation-deficient phenotype. A third gene was found to be not transcribed in vivo. A fourth gene encoded a prematurely truncated protein due to a base pair deletion that nevertheless was subject to translational frameshift repair in an Escherichia coli protein expression system. A fifth Spo0E-like protein has been structurally and functionally characterized as a phosphatase of Spo0AP by R. N. Grenha et al. (J. Biol. Chem. 281:37993-38003, 2006). We propose that these proteins may contribute to maintain B. anthracis in the transition phase of growth during an active infection and therefore contribute to the virulence of this organism.

Published ahead of print on 26 January 2007.

Supplemental material for this article may be found at http://jb.asm.org/.

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