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Endospore formation in Bacillus subtilis begins with an asymmetric cell division that partitions the bacterium into mother cell and forespore compartments. Mother cell-specific gene expression is initiated by sigmaE, a transcription factor that is active only in the mother cell but which existed as an inactive precursor (pro-sigmaE) in the predivisional cell. Activation of pro-sigmaE involves the removal of 27 amino acids from its amino terminus. A chimera of pro-sigmaE and the green fluorescent protein (GFP) was expressed from either the normal sigE promoter (P(spoIIG)), which places pro-sigmaE::GFP in both mother cell and forespore compartments, or the forespore-specific promoter (P(dacF)), which produces pro-sigmaE::GFP only in the forespore compartment. The pro-sigmaE::GFP expressed from P(spoIIG), but not P(dacF), was converted to a lower-molecular-weight form by a mechanism dependent on gene products (SpoIIGA and sigmaF) that are essential for normal pro-sigmaE processing. This finding is consistent with the pro-sigmaE processing reaction occurring only in the mother cell compartment. In processing-deficient cells, pro-sigmaE::GFP was found to accumulate at the septal membrane, a location where its processing apparatus would be susceptible to triggering from the adjoining forespore.

Bacillus subtilis Pro-sigmaE fusion protein localizes to the forespore septum and fails to be processed when synthesized in the forespore