Open AccessThe Monofunctional Glycosyltransferase of Escherichia coli Localizes to the Cell Division Site and Interacts with Penicillin-Binding Protein 3, FtsW, and FtsN
Author(s) -
Adeline Derouaux,
Benoît Wolf,
Claudine Fraipont,
Eefjan Breukink,
Martine NguyenDistèche,
Mohammed Terrak
Publication year - 2008
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.01377-07
Subject(s) - biology , escherichia coli , penicillin binding proteins , glycosyltransferase , cell division , binding site , bacterial protein , biochemistry , microbiology and biotechnology , cell , enzyme , gene
The monofunctional peptidoglycan glycosyltransferase (MtgA) catalyzes glycan chain elongation of the bacterial cell wall. Here we show that MtgA localizes at the division site ofEscherichia 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.