The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with the penicillin-binding protein 3 (PBP3), FtsW and FtsN

Adeline Derouaux; Benoît Wolf; Claudine Fraipont; E.J. Breukink; Martine Nguyen-Distèche; Mohammed Terrak

The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with the penicillin-binding protein 3 (PBP3), FtsW and FtsN

Adeline Derouaux, Benoît Wolf, Claudine Fraipont, E.J. Breukink, Martine Nguyen-Distèche, Mohammed Terrak

Dep Scheikunde

extern

Research output: Contribution to journal › Article › Academic › peer-review

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

Original language	Undefined/Unknown
Pages (from-to)	1831-1834
Number of pages	4
Journal	Journal of Bacteriology
Volume	190
Issue number	5
Publication status	Published - 2008

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title = "The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with the penicillin-binding protein 3 (PBP3), FtsW and FtsN",

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",

author = "Adeline Derouaux and Beno{\^i}t Wolf and Claudine Fraipont and E.J. Breukink and Martine Nguyen-Dist{\`e}che and Mohammed Terrak",

year = "2008",

language = "Undefined/Unknown",

volume = "190",

pages = "1831--1834",

journal = "Journal of Bacteriology",

issn = "0021-9193",

publisher = "American Society for Microbiology",

number = "5",

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The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with the penicillin-binding protein 3 (PBP3), FtsW and FtsN. / Derouaux, Adeline; Wolf, Benoît; Fraipont, Claudine et al.
In: Journal of Bacteriology, Vol. 190, No. 5, 2008, p. 1831-1834.

Research output: Contribution to journal › Article › Academic › peer-review

TY - JOUR

T1 - The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with the penicillin-binding protein 3 (PBP3), FtsW and FtsN

AU - Derouaux, Adeline

AU - Wolf, Benoît

AU - Fraipont, Claudine

AU - Breukink, E.J.

AU - Nguyen-Distèche, Martine

AU - Terrak, Mohammed

PY - 2008

Y1 - 2008

N2 - 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

AB - 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

M3 - Article

SN - 0021-9193

VL - 190

SP - 1831

EP - 1834

JO - Journal of Bacteriology

JF - Journal of Bacteriology

IS - 5

ER -