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 Katis, V. L.
Right arrow Articles by Wake, R. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Katis, V. L.
Right arrow Articles by Wake, R. G.

 Previous Article  |  Next Article 

Journal of Bacteriology, May 1999, p. 2710-2718, Vol. 181, No. 9
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Membrane-Bound Division Proteins DivIB and DivIC of Bacillus subtilis Function Solely through Their External Domains in both Vegetative and Sporulation Division

Vittorio L. Katis and R. Gerry Wake*

Department of Biochemistry, University of Sydney, Sydney, New South Wales 2006, Australia

Received 3 December 1998/Accepted 8 February 1999

The Bacillus subtilis membrane-bound division proteins, DivIB and DivIC, each contain a single transmembrane segment flanked by a short cytoplasmic N-terminal domain and a larger external C-terminal domain. Both proteins become localized at the division site prior to septation. Mutagenesis of both divIB and divIC was performed whereby the sequences encoding the cytoplasmic domains were replaced by the corresponding sequence of the other gene. Finally, the cytoplasmic-plus-transmembrane-encoding domain of each protein was replaced by a totally foreign sequence not involved in division, that encodes the N-terminal-plus-transmembrane domains of the Escherichia coli TolR protein. B. subtilis strains expressing the divIB and divIC hybrids, in the absence of the wild-type gene, were viable when grown under conditions in which the wild-type genes were found previously to be essential. Furthermore, these strains were able to sporulate to near normal levels. Thus, the cytoplasmic and transmembrane segments of DivIB and DivIC do not appear to have any specific functions other than to anchor these proteins correctly in the membrane. The implications of these findings are discussed.


* Corresponding author. Mailing address: Department of Biochemistry, University of Sydney, Sydney, New South Wales 2006, Australia. Phone: (61-2) 9351-2504. Fax: (61-2) 9351-4726. E-mail: G.Wake{at}biochem.usyd.edu.au.


Journal of Bacteriology, May 1999, p. 2710-2718, Vol. 181, No. 9
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Masson, S., Kern, T., Le Gouellec, A., Giustini, C., Simorre, J.-P., Callow, P., Vernet, T., Gabel, F., Zapun, A. (2009). Central Domain of DivIB Caps the C-terminal Regions of the FtsL/DivIC Coiled-coil Rod. J. Biol. Chem. 284: 27687-27700 [Abstract] [Full Text]  
  • Robichon, C., King, G. F., Goehring, N. W., Beckwith, J. (2008). Artificial Septal Targeting of Bacillus subtilis Cell Division Proteins in Escherichia coli: an Interspecies Approach to the Study of Protein-Protein Interactions in Multiprotein Complexes. J. Bacteriol. 190: 6048-6059 [Abstract] [Full Text]  
  • Le Gouellec, A., Roux, L., Fadda, D., Massidda, O., Vernet, T., Zapun, A. (2008). Roles of Pneumococcal DivIB in Cell Division. J. Bacteriol. 190: 4501-4511 [Abstract] [Full Text]  
  • Bennett, J. A., Aimino, R. M., McCormick, J. R. (2007). Streptomyces coelicolor Genes ftsL and divIC Play a Role in Cell Division but Are Dispensable for Colony Formation. J. Bacteriol. 189: 8982-8992 [Abstract] [Full Text]  
  • Thompson, L. S., Beech, P. L., Real, G., Henriques, A. O., Harry, E. J. (2006). Requirement for the Cell Division Protein DivIB in Polar Cell Division and Engulfment during Sporulation in Bacillus subtilis. J. Bacteriol. 188: 7677-7685 [Abstract] [Full Text]  
  • Robson, S. A., King, G. F. (2006). Domain architecture and structure of the bacterial cell division protein DivIB. Proc. Natl. Acad. Sci. USA 103: 6700-6705 [Abstract] [Full Text]  
  • Sciochetti, S. A., Lane, T., Ohta, N., Newton, A. (2002). Protein Sequences and Cellular Factors Required for Polar Localization of a Histidine Kinase in Caulobacter crescentus. J. Bacteriol. 184: 6037-6049 [Abstract] [Full Text]  
  • Chen, J. C., Minev, M., Beckwith, J. (2002). Analysis of ftsQ Mutant Alleles in Escherichia coli: Complementation, Septal Localization, and Recruitment of Downstream Cell Division Proteins. J. Bacteriol. 184: 695-705 [Abstract] [Full Text]  
  • Sievers, J., Errington, J. (2000). Analysis of the Essential Cell Division Gene ftsL of Bacillus subtilis by Mutagenesis and Heterologous Complementation. J. Bacteriol. 182: 5572-5579 [Abstract] [Full Text]  
  • Katis, V. L., Wake, R. G., Harry, E. J. (2000). Septal Localization of the Membrane-Bound Division Proteins of Bacillus subtilis DivIB and DivIC Is Codependent Only at High Temperatures and Requires FtsZ. J. Bacteriol. 182: 3607-3611 [Abstract] [Full Text]