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J. Bacteriol. doi:10.1128/JB.00992-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

A role for the non-essential N-terminus of FtsN in divisome assembly

Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115 U.S.A.

^* To whom correspondence should be addressed. Email: jon_beckwith{at}hms.harvard.edu.

	Abstract

FtsN, the last essential protein in the cell division localization hierarchy in Escherichia coli, exhibits several peculiar characteristics suggesting that it has a unique role in the division process despite its being conserved only among 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 have examined the requirements for this phenomenon. We find 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.

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