ORBi: Derouaux Adeline - The Monofunctional Glycosyltransferase of Escherichia Coli Localizes to the Cell Division Site and Interacts with Penicillin-Binding Protein 3, FtsW, and FtsN

Reference : The Monofunctional Glycosyltransferase of Escherichia Coli Localizes to the Cell Divisio...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/15090

Title :	The Monofunctional Glycosyltransferase of Escherichia Coli Localizes to the Cell Division Site and Interacts with Penicillin-Binding Protein 3, FtsW, and FtsN
Language :	English
Author, co-author :	Derouaux, Adeline [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
	Wolf, Benoît [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
	Fraipont, Claudine [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
	Breukink, Eefjan [Universiteit Utrecht > > >Department of Biochemistry of Membranes > > > >]
	Nguyen-Disteche, Martine [Université de Liège - ULG > >Centre d'Ingénierie des protéines > > > > >]
	Terrak, Mohammed [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Publication date :	Mar-2008
Journal title :	Journal of Bacteriology
Publisher :	American Society for Microbiology (ASM)
Volume :	190
Issue/season :	5
Pages :	1831-4
Peer reviewed :	Yes (verified by ORBi)
Audience :	International
ISSN :	0021-9193
e-ISSN :	1098-5530
City :	Washington
Country :	DC
Abstract :	[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.
Target :	Researchers
Permalink :	http://hdl.handle.net/2268/15090
DOI :	10.1128/JB.01377-07

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