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Journal of Bacteriology, December 2009, p. 7383-7401, Vol. 191, No. 24
0021-9193/09/$08.00+0     doi:10.1128/JB.00811-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Self-Enhanced Accumulation of FtsN at Division Sites and Roles for Other Proteins with a SPOR Domain (DamX, DedD, and RlpA) in Escherichia coli Cell Constriction {triangledown} ,{dagger}

Matthew A. Gerding,{ddagger} Bing Liu,{ddagger} Felipe O. Bendezú,{ddagger},§ Cynthia A. Hale, Thomas G. Bernhardt, and Piet A. J. de Boer*

Department of Molecular Biology & Microbiology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106-4960

Received 22 June 2009/ Accepted 6 August 2009

Of the known essential division proteins in Escherichia coli, FtsN is the last to join the septal ring organelle. FtsN is a bitopic membrane protein with a small cytoplasmic portion and a large periplasmic one. The latter is thought to form an {alpha}-helical juxtamembrane region, an unstructured linker, and a C-terminal, globular, murein-binding SPOR domain. We found that the essential function of FtsN is accomplished by a surprisingly small essential domain (EFtsN) of at most 35 residues that is centered about helix H2 in the periplasm. EFtsN contributed little, if any, to the accumulation of FtsN at constriction sites. However, the isolated SPOR domain (SFtsN) localized sharply to these sites, while SPOR-less FtsN derivatives localized poorly. Interestingly, localization of SFtsN depended on the ability of cells to constrict and, thus, on the activity of EFtsN. This and other results suggest that, compatible with a triggering function, FtsN joins the division apparatus in a self-enhancing fashion at the time of constriction initiation and that its SPOR domain specifically recognizes some form of septal murein that is only transiently available during the constriction process. SPOR domains are widely distributed in bacteria. The isolated SPOR domains of three additional E. coli proteins of unknown function, DamX, DedD, and RlpA, as well as that of Bacillus subtilis CwlC, also accumulated sharply at constriction sites in E. coli, suggesting that septal targeting is a common property of SPORs. Further analyses showed that DamX and, especially, DedD are genuine division proteins that contribute significantly to the cell constriction process.

* Corresponding author. Mailing address: Department of Molecular Biology & Microbiology, School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, OH 44106-4960. Phone: (216) 368-1697. Fax: (216) 368-3055. E-mail: pad5{at}po.cwru.edu

{triangledown} Published ahead of print on 14 August 2009.

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

{ddagger} M.A.G., B.L., and F.O.B. contributed equally to this study.

§ Present address: Center for Integrative Genomics, University of Lausanne, Lausanne, Switzerland.

Present address: Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA.

Journal of Bacteriology, December 2009, p. 7383-7401, Vol. 191, No. 24
0021-9193/09/$08.00+0     doi:10.1128/JB.00811-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Related articles in JB:

FtsN—Trigger for Septation
Joe Lutkenhaus
JB 2009 191: 7381-7382. [Full Text]  



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  • Lutkenhaus, J. (2009). FtsN--Trigger for Septation. J. Bacteriol. 191: 7381-7382 [Full Text]  


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