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Vol. 180, Issue 13, 3276-3284, July 1, 1998

Establishment of Prespore-Specific Gene Expression in Bacillus subtilis: Localization of SpoIIE Phosphatase and Initiation of Compartment-Specific Proteolysis

Peter J. Lewis, Ling Juan Wu, and Jeffery Errington

Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom

Immunofluorescence microscopy was used to study the establishment of compartment-specific transcription during sporulation in Bacillus subtilis. Analysis of the distribution of the anti-anti-sigma factor, SpoIIAA, in a variety of mutant backgrounds supports a model in which the SpoIIE phosphatase, which activates SpoIIAA by dephosphorylation, is sequestered onto the prespore face of the asymmetric septum. Thus, prespore-specific gene expression apparently arises as a result of the compartmentalization of SpoIIE protein. The results also suggest the existence of at least two compartment-specific programs of proteolysis, one dependent on the mother cell-specific sigma factor sigma E and the other dependent on the prespore-specific sigma factor sigma F.

Copyright © 1998 by American Society for Microbiology


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