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Journal of Bacteriology, October 2004, p. 6728-6737, Vol. 186, No. 20
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.20.6728-6737.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Murein (Peptidoglycan) Binding Property of the Essential Cell Division Protein FtsN from Escherichia coli

Astrid Ursinus,1,{dagger} Fusinita van den Ent,2 Sonja Brechtel,1 Miguel de Pedro,3 Joachim-Volker Höltje,1,{ddagger} Jan Löwe,2 and Waldemar Vollmer1*

Universität Tübingen, Fakultät für Biologie, Lehrbereich Mikrobielle Genetik, Tübingen, Germany,1 M.R.C. Laboratory of Molecular Biology, Cambridge, United Kingdom,2 Facultad de Ciencias UAM, Campus de Cantoblanco, Centro de Biología Molecular "Severo Ochoa" CSIC-UAM, Madrid, Spain3

Received 30 March 2004/ Accepted 15 July 2004

The binding of the essential cell division protein FtsN of Escherichia coli to the murein (peptidoglycan) sacculus was studied. Soluble truncated variants of FtsN, including the complete periplasmic part of the protein as well as a variant containing only the C-terminal 77 amino acids, did bind to purified murein sacculi isolated from wild-type cells. FtsN variants lacking this C-terminal region showed reduced or no binding to murein. Binding of FtsN was severely reduced when tested against sacculi isolated either from filamentous cells with blocked cell division or from chain-forming cells of a triple amidase mutant. Binding experiments with radioactively labeled murein digestion products revealed that the longer murein glycan strands (>25 disaccharide units) showed a specific affinity to FtsN, but neither muropeptides, peptides, nor short glycan fragments bound to FtsN. In vivo FtsN could be cross-linked to murein with the soluble disulfide bridge containing cross-linker DTSSP. Less FtsN, but similar amounts of OmpA, was cross-linked to murein of filamentous or of chain-forming cells compared to levels in wild-type cells. Expression of truncated FtsN variants in cells depleted in full-length FtsN revealed that the presence of the C-terminal murein-binding domain was not required for cell division under laboratory conditions. FtsN was present in 3,000 to 6,000 copies per cell in exponentially growing wild-type E. coli MC1061. We discuss the possibilities that the binding of FtsN to murein during cell division might either stabilize the septal region or might have a function unrelated to cell division.

* Corresponding author. Mailing address: Universität Tübingen, Fakultät für Biologie, Lehrbereich Mikrobielle Genetik, Auf der Morgenstelle 28, 72076 Tübingen, Germany. Phone: 49-7071-2974635. Fax: 49-7071-295065. E-mail: waldemar.vollmer{at}uni-tuebingen.de.

{dagger} Present address: Max-Planck-Institut für Entwicklungsbiologie, Abteilung Protein Evolution, 72076 Tübingen, Germany.

{ddagger} Present address: Galerie Jochen Höltje, Tübingen, 72072 Tübingen, Germany.

Journal of Bacteriology, October 2004, p. 6728-6737, Vol. 186, No. 20
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.20.6728-6737.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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