PMID:18165305
| Citation |
Derouaux, A, Wolf, B, Fraipont, C, Breukink, E, Nguyen-Distèche, M and Terrak, M (2008) The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillin-binding protein 3, FtsW, and FtsN. J. Bacteriol. 190:1831-4 |
|---|---|
| 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. |
| Links |
PubMed PMC2258671 Online version:10.1128/JB.01377-07 |
| Keywords |
Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Green Fluorescent Proteins/genetics; Green Fluorescent Proteins/metabolism; Membrane Proteins/genetics; Membrane Proteins/metabolism; Microscopy, Fluorescence; Penicillin-Binding Proteins/genetics; Penicillin-Binding Proteins/metabolism; Peptidoglycan Glycosyltransferase/genetics; Peptidoglycan Glycosyltransferase/metabolism; Protein Binding; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Serine-Type D-Ala-D-Ala Carboxypeptidase/genetics; Serine-Type D-Ala-D-Ala Carboxypeptidase/metabolism; Two-Hybrid System Techniques |
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