This Article Full Text Full Text (PDF) Other Versions of this Article: JB.01347-06v1 189/1/98    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Reddy, M. Search for Related Content PubMed PubMed Citation Articles by Reddy, M.

 Previous Article  |  Next Article 

Journal of Bacteriology, January 2007, p. 98-108, Vol. 189, No. 1
0021-9193/07/$08.00+0     doi:10.1128/JB.01347-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Role of FtsEX in Cell Division of Escherichia coli: Viability of ftsEX Mutants Is Dependent on Functional SufI or High Osmotic Strength

Centre for Cellular and Molecular Biology, Hyderabad 500007, India

Received 24 August 2006/ Accepted 16 October 2006

In Escherichia coli, at least 12 proteins, FtsZ, ZipA, FtsA, FtsE/X, FtsK, FtsQ, FtsL, FtsB, FtsW, FtsI, FtsN, and AmiC, are known to localize to the septal ring in an interdependent and sequential pathway to coordinate the septum formation at the midcell. The FtsEX complex is the latest recruit of this pathway, and unlike other division proteins, it is shown to be essential only on low-salt media. In this study, it is shown that ftsEX null mutations are not only salt remedial but also osmoremedial, which suggests that FtsEX may not be involved in salt transport as previously thought. Increased coexpression of cell division proteins FtsQ-FtsA-FtsZ or FtsN alone restored the growth defects of ftsEX mutants. ftsEX deletion exacerbated the defects of most of the mutants affected in Z ring localization and septal assembly; however, the ftsZ84 allele was a weak suppressor of ftsEX. The viability of ftsEX mutants in high-osmolarity conditions was shown to be dependent on the presence of a periplasmic protein, SufI, a substrate of twin-arginine translocase. In addition, SufI in multiple copies could substitute for the functions of FtsEX. Taken together, these results suggest that FtsE and FtsX are absolutely required for the process of cell division in conditions of low osmotic strength for the stability of the septal ring assembly and that, during high-osmolarity conditions, the FtsEX and SufI functions are redundant for this essential process.

Published ahead of print on 27 October 2006.

This article has been cited by other articles:

• 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]  
• Hett, E. C., Rubin, E. J. (2008). Bacterial Growth and Cell Division: a Mycobacterial Perspective. Microbiol. Mol. Biol. Rev. 72: 126-156 [Abstract] [Full Text]  
• Samaluru, H., SaiSree, L., Reddy, M. (2007). Role of SufI (FtsP) in Cell Division of Escherichia coli: Evidence for Its Involvement in Stabilizing the Assembly of the Divisome. J. Bacteriol. 189: 8044-8052 [Abstract] [Full Text]  
• Fujiwara, K., Taguchi, H. (2007). Filamentous Morphology in GroE-Depleted Escherichia coli Induced by Impaired Folding of FtsE. J. Bacteriol. 189: 5860-5866 [Abstract] [Full Text]  
• Corbin, B. D., Wang, Y., Beuria, T. K., Margolin, W. (2007). Interaction between Cell Division Proteins FtsE and FtsZ. J. Bacteriol. 189: 3026-3035 [Abstract] [Full Text]