This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ju, J.
Right arrow Articles by Haldenwang, W. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ju, J.
Right arrow Articles by Haldenwang, W. G.

 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.

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

Jingliang Ju{dagger} 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

{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.


* Corresponding author. Mailing address: Dept. of Microbiology & Immunology MC7758, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Dr., San Antonio, TX 78229-3900. Phone: (210) 567-3957. Fax: (210) 567-6612. E-mail: Haldenwang{at}UTHSCSA.EDU.

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


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.




This article has been cited by other articles:

  • Imamura, D., Zhou, R., Feig, M., Kroos, L. (2008). Evidence That the Bacillus subtilis SpoIIGA Protein Is a Novel Type of Signal-transducing Aspartic Protease. J. Biol. Chem. 283: 15287-15299 [Abstract] [Full Text]  
  • Hilbert, D. W., Piggot, P. J. (2004). Compartmentalization of Gene Expression during Bacillus subtilis Spore Formation. Microbiol. Mol. Biol. Rev. 68: 234-262 [Abstract] [Full Text]  
  • McBride, S., Haldenwang, W. G. (2004). Sporulation Phenotype of a Bacillus subtilis Mutant Expressing an Unprocessable but Active {sigma}E Transcription Factor. J. Bacteriol. 186: 1999-2005 [Abstract] [Full Text]