The Monofunctional Glycosyltransferase of Escherichia Coli Localizes to the Cell Division Site and Interacts with Penicillin-Binding Protein 3, FtsW, and FtsN
[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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Derouaux, Adeline ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Wolf, Benoît ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Fraipont, Claudine ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Breukink, Eefjan; Universiteit Utrecht > Department of Biochemistry of Membranes
Terrak, Mohammed ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Language :
English
Title :
The Monofunctional Glycosyltransferase of Escherichia Coli Localizes to the Cell Division Site and Interacts with Penicillin-Binding Protein 3, FtsW, and FtsN
Publication date :
March 2008
Journal title :
Journal of Bacteriology
ISSN :
0021-9193
eISSN :
1098-5530
Publisher :
American Society for Microbiology (ASM), Washington, United States - District of Columbia
