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J Bacteriol. 2008 Mar;190(5):1831-4. doi: 10.1128/JB.01377-07. Epub 2007 Dec 28.

The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillin-binding protein 3, FtsW, and FtsN.

Author information

  • 1Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, B6a, B-4000 Sart-Tilman (Liège), Belgium.

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.

PMID:
18165305
[PubMed - indexed for MEDLINE]
PMCID:
PMC2258671
Free PMC Article
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