JB Accepts, published online ahead of print on 28 December 2007

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J. Bacteriol. doi:10.1128/JB.01377-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with the penicillin-binding protein 3 (PBP3), FtsW and FtsN

Adeline Derouaux, Benoît Wolf, Claudine Fraipont, Eefjan Breukink, Martine Nguyen-Distèche, and Mohammed Terrak^*

Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, B6a, B-4000 Sart-Tilman (Liège), Belgium; Department of Biochemistry of Membranes, Bijvoet Center for Biomolecular Research, Institute of Biomembranes, Utrecht University, Padualaan, 8, 3584 CH, Utrecht, The Netherlands

^* To whom correspondence should be addressed. Email: mterrak{at}ulg.ac.be.

The monofunctional peptidoglycan glycosyltransferase (MtgA) catalyses glycan chain elongation of the bacterial cell wall. Here we show that MtgA localizes at the division site of Escherichia coli deficient in PBP1b and producing a thermosensitive PBP1a and is able to interact with three constituents of the divisome, PBP3, FtsW and FtsN suggesting that MtgA may play a role in peptidogl ycan assembly during the cell cycle in collaboration with other proteins.

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