Reference : The Monofunctional Glycosyltransferase of Escherichia Coli Localizes to the Cell Divisio...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/15090
The Monofunctional Glycosyltransferase of Escherichia Coli Localizes to the Cell Division Site and Interacts with Penicillin-Binding Protein 3, FtsW, and FtsN
English
Derouaux, Adeline mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Wolf, Benoît mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Fraipont, Claudine mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Breukink, Eefjan mailto [Universiteit Utrecht > > >Department of Biochemistry of Membranes > > > >]
Nguyen-Disteche, Martine mailto [Université de Liège - ULG > >Centre d'Ingénierie des protéines > > > > >]
Terrak, Mohammed mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Mar-2008
Journal of Bacteriology
American Society for Microbiology (ASM)
190
5
1831-4
Yes (verified by ORBi)
International
0021-9193
1098-5530
Washington
DC
[en] 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.
Researchers
http://hdl.handle.net/2268/15090
10.1128/JB.01377-07

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