This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
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 Campo, N.
Right arrow Articles by Rudner, D. Z.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Campo, N.
Right arrow Articles by Rudner, D. Z.

 Previous Article  |  Next Article 

Journal of Bacteriology, August 2007, p. 6021-6027, Vol. 189, No. 16
0021-9193/07/$08.00+0     doi:10.1128/JB.00399-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

SpoIVB and CtpB Are Both Forespore Signals in the Activation of the Sporulation Transcription Factor {sigma}K in Bacillus subtilis{triangledown} ,{dagger}

Nathalie Campo and David Z. Rudner*

Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115

Received 16 March 2007/ Accepted 29 May 2007

The proteolytic activation of the mother cell transcription factor pro-{sigma}K is controlled by a signal transduction pathway during sporulation in the bacterium Bacillus subtilis. The pro-{sigma}K processing enzyme SpoIVFB, a membrane-embedded metalloprotease, is held inactive by two other integral membrane proteins, SpoIVFA and BofA, in the mother cell membrane that surrounds the forespore. Two signaling serine proteases, SpoIVB and CtpB, trigger pro-{sigma}K processing by cleaving the regulatory protein SpoIVFA. The SpoIVB signal is absolutely required to activate pro-{sigma}K processing and is derived from the forespore compartment. CtpB is necessary for the proper timing of {sigma}K activation and was thought to be a mother cell signal. Here, we show that the ctpB gene is expressed in both the mother cell and forespore compartments but that synthesis in the forespore under the control of {sigma}G is both necessary and sufficient for the proper timing of pro-{sigma}K processing. We further show that SpoIVB cleaves CtpB in vitro and in vivo but that this cleavage does not appear to be necessary for CtpB activation. Thus, both signaling proteins are made in the forespore and independently target the same regulatory protein.


* Corresponding author. Mailing address: Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Ave., Boston, MA 02115. Phone: (617) 432-4455. Fax: (617) 738-7664. E-mail: rudner{at}hms.harvard.edu

{triangledown} Published ahead of print on 8 June 2007.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.


Journal of Bacteriology, August 2007, p. 6021-6027, Vol. 189, No. 16
0021-9193/07/$08.00+0     doi:10.1128/JB.00399-07
Copyright © 2007, 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]  
  • Campo, N., Marquis, K. A., Rudner, D. Z. (2008). SpoIIQ Anchors Membrane Proteins on Both Sides of the Sporulation Septum in Bacillus subtilis. J. Biol. Chem. 283: 4975-4982 [Abstract] [Full Text]