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M706390200v1
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Papers In Press, published online ahead of print October 15, 2007
J. Biol. Chem, 10.1074/jbc.M706390200
Submitted on August 2, 2007
Accepted on October 15, 2007

The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli

Patrick Müller, Carolin Ewers, Ute Bertsche, Maria Anstett, Tanja Kallis, Eefjan Breukink, Claudine Fraipont, Mohammed Terrak, Martine Nguyen-Distèche, and Waldemar Vollmer

Institute for Cell and Molecular Biosciences, Newcastle upon Tyne NE2 4HH

Corresponding Author: w.vollmer{at}ncl.ac.uk

Bacterial cell division requires the co-ordinated 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 pull-down 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.


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