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

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2008

Authors

Derouaux, Adeline
Wolf, Benoît
Fraipont, Claudine
Breukink, EefjanISNI 0000000392861563
Nguyen-Distèche, Martine
Terrak, Mohammed

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Article

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Utrecht University Repository

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Abstract

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

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International (English)

Citation

Derouaux, A, Wolf, B, Fraipont, C, Breukink, E J, Nguyen-Distèche, M & Terrak, M 2008, 'The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with the penicillin-binding protein 3 (PBP3), FtsW and FtsN', Journal of Bacteriology, vol. 190, no. 5, pp. 1831-1834.

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http://hdl.handle.net/1874/43920