Tethering of the Bacillus subtilis sigma E proprotein to the cell membrane is necessary for its processing but insufficient for its stabilization.

Abstract

sigma(E), a sporulation-specific transcription factor of Bacillus subtilis, is synthesized as an inactive proprotein with a 27-amino acid extension at its amino terminus. This "pro" sequence is removed by a developmentally regulated protease, but when present, it blocks sigma(E) activity, tethers sigma(E) to the bacterium's cytoplasmic membrane, and promotes sigma(E) stability. To investigate whether pro-sigma(E) processing and/or stabilization are tied to membrane sequestration, we used fluorescent protein fusions to examine the membrane binding of SigE variants. The results are consistent with membrane association as a prerequisite for pro-sigma(E) processing but not as a sufficient cause for the proprotein's stability.