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J. Biol. Chem., Vol. 282, Issue 50, 36394-36402, December 14, 2007

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The Essential Cell Division Protein FtsN Interacts with the Murein (Peptidoglycan) Synthase PBP1B in Escherichia coli^*

Patrick Müller¹, Carolin Ewers¹², Ute Bertsche¹, Maria Anstett, Tanja Kallis³, Eefjan Breukink, Claudine Fraipont^¶, Mohammed Terrak^¶, Martine Nguyen-Distèche^¶, and Waldemar Vollmer⁴

From the Microbial Genetics, University of Tübingen, 72076 Tübingen, Germany, Center of Biomembranes and Lipid Enzymology, Department of Biochemistry of Membranes, Institute for Biomembranes, University of Utrecht, 3584 CH Utrecht, The Netherlands, and ^¶Centre d'Ingénierie des Protéines, Institut de Chimie B6a, Université de Liège, B-4000 Sart Tilman, Belgium

Bacterial cell division requires the coordinated action of cell division proteins and murein (peptidoglycan) synthases. Interactions involving the essential cell division protein FtsN and murein synthases were studied by affinity chromatography with membrane fraction. The murein synthases PBP1A, PBP1B, and PBP3 had an affinity to immobilized FtsN. FtsN and PBP3, but not PBP1A, showed an affinity to immobilized PBP1B. The direct interaction between FtsN and PBP1B was confirmed by pulldown experiments and surface plasmon resonance. The interaction was also detected by bacterial two-hybrid analysis. FtsN and PBP1B could be cross-linked in intact cells of the wild type and in cells depleted of PBP3 or FtsW. FtsN stimulated the in vitro murein synthesis activities of PBP1B. Thus, FtsN could have a role in controlling or modulating the activity of PBP1B during cell division in Escherichia coli.

Received for publication, August 2, 2007 , and in revised form, September 28, 2007.

^* This work was supported by the Deutsche Forschungsgemeinschaft within the Forschergruppe Bakterielle Zellhülle (FOR 449), the European Commission within the EUR-INTAFAR (LSHM-CT-2004-512138) network and the Belgian State, Prime Minister's Office, Science Policy programming (IAP number P6/19), the Actions de Recherche Concertées (Grant 03/08-297). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ These authors contributed equally to this work.

² Present address: Dept. of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.

³ Present address: steripac GmbH, Calw-Altburg, Germany.

⁴ To whom correspondence should be addressed: Inst. for Cell and Molecular Biosciences, Medical School, University of Newcastle upon Tyne, Catherine Cookson Bldg., Framlington Place, Newcastle upon Tyne NE2 4HH, UK. Tel.: 44-191-222-6295; Fax: 44-191-222-7424; E-mail: W.Vollmer{at}ncl.ac.uk.

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