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