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Tethering of the Bacillus subtilis ^E Proprotein to the Cell Membrane Is Necessary for Its Processing but Insufficient for Its Stabilization

Jingliang Ju and W. G. Haldenwang^*

Department of Microbiology & Immunology, University of Texas Health Science Center, San Antonio, Texas 78229-3900

Received 8 May 2003/ Accepted 7 July 2003

^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 ^E activity, tethers ^E to the bacterium's cytoplasmic membrane, and promotes ^E stability. To investigate whether pro-^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-^E processing but not as a sufficient cause for the proprotein's stability.

Present address: Adaptive Therapeutics, Inc., San Diego, CA 92121.

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