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Journal of Bacteriology, October 2005, p. 6972-6981, Vol. 187, No. 20
0021-9193/05/$08.00+0     doi:10.1128/JB.187.20.6972-6981.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Characterization of Sporulation Histidine Kinases of Bacillus anthracis{dagger} ,{ddagger}

Ryan L. Brunsing, Chandra La Clair, Sharon Tang, Christina Chiang, Lynn E. Hancock, Marta Perego, and James A. Hoch*

The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, California 92037

Received 5 May 2005/ Accepted 20 July 2005

The initiation of sporulation in Bacillus species is regulated by the phosphorelay signal transduction pathway, which is activated by several histidine sensor kinases in response to cellular and metabolic signals. Comparison of the protein components of the phosphorelay between Bacillus subtilis and Bacillus anthracis revealed high homology in the phosphorelay orthologs of Spo0F, Spo0B, and Spo0A. The sensor domains of sensor histidine kinases are poorly conserved between species, making ortholog recognition tenuous. Putative sporulation sensor histidine kinases of B. anthracis were identified by homology to the HisKA domain of B. subtilis sporulation sensor histidine kinases, which interacts with Spo0F. Nine possible kinases were uncovered, and their genes were assayed for complementation of kinase mutants of B. subtilis, for ability to drive lacZ expression in B. subtilis and B. anthracis, and for the effect of deletion of each on the sporulation of B. anthracis. Five of the nine sensor histidine kinases were inferred to be capable of inducing sporulation in B. anthracis. Four of the sensor kinases could not be shown to induce sporulation; however, the genes for two of these were frameshifted in all B. anthracis strains and one of these was also frameshifted in the pathogenic pXO1-bearing Bacillus cereus strain G9241. It is proposed that acquisition of plasmid pXO1 and pathogenicity may require a dampening of sporulation regulation by mutational selection of sporulation sensor histidine kinase defects. The sporulation of B. anthracis ex vivo appears to result from any one or a combination of the sporulation sensor histidine kinases remaining.

* Corresponding author. Mailing address: Division of Cellular Biology, Mail Code MEM-116, Department of Molecular and Experimental Medicine, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037. Phone: (858) 784-7905. Fax: (858) 784-7966. E-mail: hoch{at}scripps.edu.

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

{ddagger} Paper no. 17150-MEM from The Scripps Research Institute.

Journal of Bacteriology, October 2005, p. 6972-6981, Vol. 187, No. 20
0021-9193/05/$08.00+0     doi:10.1128/JB.187.20.6972-6981.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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