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Journal of Bacteriology, April 2009, p. 2815-2825, Vol. 191, No. 8
0021-9193/09/$08.00+0     doi:10.1128/JB.01597-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Divisome under Construction: Distinct Domains of the Small Membrane Protein FtsB Are Necessary for Interaction with Multiple Cell Division Proteins {triangledown} ,{dagger}

Mark D. Gonzalez and Jon Beckwith*

Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, Massachusetts 02115

Received 11 November 2008/ Accepted 10 February 2009

Cell division in bacteria requires the coordinated action of a set of proteins, the divisome, for proper constriction of the cell envelope. Multiple protein-protein interactions are required for assembly of a stable divisome. Within the Escherichia coli divisome is a conserved subcomplex of inner membrane proteins, the FtsB/FtsL/FtsQ complex, which is necessary for linking the upstream division proteins, which are predominantly cytoplasmic, with the downstream division proteins, which are predominantly periplasmic. FtsB and FtsL are small bitopic membrane proteins with predicted coiled-coil motifs, which themselves form a stable subcomplex that can recruit downstream division proteins independently of FtsQ; however, the details of how FtsB and FtsL interact together and with other proteins remain to be characterized. Despite the small size of FtsB, we identified separate interaction domains of FtsB that are required for interaction with FtsL and FtsQ. The N-terminal half of FtsB is necessary for interaction with FtsL and sufficient, when in complex with FtsL, for recruitment of downstream division proteins, while a portion of the FtsB C terminus is necessary for interaction with FtsQ. These properties of FtsB support the proposal that its main function is as part of a molecular scaffold to allow for proper formation of the divisome.

* Corresponding author. Mailing address: Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115. Phone: (617) 432-1920. Fax: (617) 738-7664. E-mail: jon_beckwith{at}hms.harvard.edu

{triangledown} Published ahead of print on 20 February 2009.

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

Journal of Bacteriology, April 2009, p. 2815-2825, Vol. 191, No. 8
0021-9193/09/$08.00+0     doi:10.1128/JB.01597-08
Copyright © 2009, 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]  
  • 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]  


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