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Journal of Bacteriology, January 2007, p. 646-649, Vol. 189, No. 2
0021-9193/07/$08.00+0     doi:10.1128/JB.00992-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Role for the Nonessential N Terminus of FtsN in Divisome Assembly{triangledown}

Nathan W. Goehring, Carine Robichon, and Jon Beckwith*

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

Received 6 July 2006/ Accepted 10 October 2006

FtsN, the last essential protein in the cell division localization hierarchy in Escherichia coli, has several peculiar characteristics, suggesting that it has a unique role in the division process despite the fact that it is conserved in only a subset of bacteria. In addition to suppressing temperature-sensitive mutations in ftsA, ftsK, ftsQ, and ftsI, overexpression of FtsN can compensate for a complete lack of FtsK in the cell. We examined the requirements for this phenomenon. We found that the N-terminal terminal region (cytoplasmic and transmembrane domains) is critical for suppression, while the C-terminal murein-binding domain is dispensable. Our results further suggest that FtsN and FtsK act cooperatively to stabilize 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 27 October 2006.

Journal of Bacteriology, January 2007, p. 646-649, Vol. 189, No. 2
0021-9193/07/$08.00+0     doi:10.1128/JB.00992-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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