Previous Article | Next Article ![]()
Journal of Bacteriology, October 2003, p. 5897-5900, Vol. 185, No. 19
0021-9193/03/$08.00+0 DOI: 10.1128/JB.185.19.5897-5900.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
E Proprotein to the Cell Membrane Is Necessary for Its Processing but Insufficient for Its Stabilization
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.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»