| Literature DB >> 18165305 |
Adeline Derouaux1, Benoît Wolf, Claudine Fraipont, Eefjan Breukink, Martine Nguyen-Distèche, Mohammed Terrak.
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.Entities:
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Year: 2007 PMID: 18165305 PMCID: PMC2258671 DOI: 10.1128/JB.01377-07
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490