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 Jensen, S. O.
Right arrow Articles by Harry, E. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jensen, S. O.
Right arrow Articles by Harry, E. J.

 Previous Article  |  Next Article 

Journal of Bacteriology, September 2005, p. 6536-6544, Vol. 187, No. 18
0021-9193/05/$08.00+0     doi:10.1128/JB.187.18.6536-6544.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Cell Division in Bacillus subtilis: FtsZ and FtsA Association Is Z-Ring Independent, and FtsA Is Required for Efficient Midcell Z-Ring Assembly

S. O. Jensen,1,{dagger} L. S. Thompson,2 and E. J. Harry2*

School of Molecular and Microbial Biosciences, University of Sydney, Sydney, New South Wales 2006, Australia,1 Institute for the Biotechnology of Infectious Diseases, University of Technology, Sydney, New South Wales 2007, Australia2

Received 27 January 2005/ Accepted 5 May 2005

The earliest stage in cell division in bacteria is the assembly of a Z ring at the division site at midcell. Other division proteins are also recruited to this site to orchestrate the septation process. FtsA is a cytosolic division protein that interacts directly with FtsZ. Its function remains unknown. It is generally believed that FtsA localization to the division site occurs immediately after Z-ring formation or concomitantly with it and that FtsA is responsible for recruiting the later-assembling membrane-bound division proteins to the division site. Here, we report the development of an in vivo chemical cross-linking assay to examine the association between FtsZ and FtsA in Bacillus subtilis cells. We subsequently use this assay in a synchronous cell cycle to show that these two proteins can interact prior to Z-ring formation. We further show that in a B. subtilis strain containing an ftsA deletion, FtsZ localized at regular intervals along the filament but the majority of Z rings were abnormal. FtsA in this organism is therefore critical for the efficient formation of functional Z rings. This is the first report of abnormal Z-ring formation resulting from the loss of a single septation protein. These results suggest that in this organism, and perhaps others, FtsA ensures recruitment of the membrane-bound division proteins by ensuring correct formation of the Z ring.

* Corresponding author. Mailing address: Institute for the Biotechnology of Infectious Diseases, University of Technology, Sydney, NSW 2007, Australia. Phone: 61 2 9514 4173. Fax: 61 2 9514 4201. E-mail: liz.harry{at}uts.edu.au.

{dagger} Present address: School of Biological Sciences, University of Sydney, Sydney, NSW 2006, Australia.

Journal of Bacteriology, September 2005, p. 6536-6544, Vol. 187, No. 18
0021-9193/05/$08.00+0     doi:10.1128/JB.187.18.6536-6544.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Gamba, P., Veening, J.-W., Saunders, N. J., Hamoen, L. W., Daniel, R. A. (2009). Two-Step Assembly Dynamics of the Bacillus subtilis Divisome. J. Bacteriol. 191: 4186-4194 [Abstract] [Full Text]  
  • Beuria, T. K., Mullapudi, S., Mileykovskaya, E., Sadasivam, M., Dowhan, W., Margolin, W. (2009). Adenine Nucleotide-dependent Regulation of Assembly of Bacterial Tubulin-like FtsZ by a Hypermorph of Bacterial Actin-like FtsA. J. Biol. Chem. 284: 14079-14086 [Abstract] [Full Text]  
  • Singh, J. K., Makde, R. D., Kumar, V., Panda, D. (2008). SepF Increases the Assembly and Bundling of FtsZ Polymers and Stabilizes FtsZ Protofilaments by Binding along Its Length. J. Biol. Chem. 283: 31116-31124 [Abstract] [Full Text]  
  • Tavares, J. R., de Souza, R. F., Meira, G. L. S., Gueiros-Filho, F. J. (2008). Cytological Characterization of YpsB, a Novel Component of the Bacillus subtilis Divisome. J. Bacteriol. 190: 7096-7107 [Abstract] [Full Text]  
  • Geissler, B., Shiomi, D., Margolin, W. (2007). The ftsA* gain-of-function allele of Escherichia coli and its effects on the stability and dynamics of the Z ring. Microbiology 153: 814-825 [Abstract] [Full Text]  
  • Shiomi, D., Margolin, W. (2007). The C-Terminal Domain of MinC Inhibits Assembly of the Z Ring in Escherichia coli. J. Bacteriol. 189: 236-243 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»