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Journal of Bacteriology, March 2008, p. 1831-1834, Vol. 190, No. 5
0021-9193/08/$08.00+0     doi:10.1128/JB.01377-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

The Monofunctional Glycosyltransferase of Escherichia coli Localizes to the Cell Division Site and Interacts with Penicillin-Binding Protein 3, FtsW, and FtsN{triangledown} ,{ddagger}

Adeline Derouaux,1,{dagger} Benoît Wolf,1,{dagger} Claudine Fraipont,1 Eefjan Breukink,2 Martine Nguyen-Distèche,1 and Mohammed Terrak1*

Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, B6a, B-4000 Sart-Tilman (Liège), Belgium,1 Department of Biochemistry of Membranes, Bijvoet Center for Biomolecular Research, Institute of Biomembranes, Utrecht University, Padualaan, 8, 3584 CH, Utrecht, The Netherlands2

Received 24 August 2007/ Accepted 15 December 2007

The monofunctional peptidoglycan glycosyltransferase (MtgA) catalyzes glycan chain elongation of the bacterial cell wall. Here we show that MtgA localizes at the division site of Escherichia coli cells that are deficient in PBP1b and produce 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 peptidoglycan assembly during the cell cycle in collaboration with other proteins.

* Corresponding author. Mailing address: Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, B6a, B-4000 Sart-Tilman (Liège), Belgium. Phone: 32-4-3663397. Fax: 32-4-3663364. E-mail: mterrak{at}ulg.ac.be

{triangledown} Published ahead of print on 28 December 2007.

{ddagger} Supplemental material for this article may be found at http://jb.asm.org/.

{dagger} These authors contributed equally to this work.

Journal of Bacteriology, March 2008, p. 1831-1834, Vol. 190, No. 5
0021-9193/08/$08.00+0     doi:10.1128/JB.01377-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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