Article (Scientific journals)
The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli
Muller, P.; Ewers, C.; Bertsche, U. et al.
2007In Journal of Biological Chemistry, 282 (50), p. 36394-36402
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Abstract :
[en] Bacterial cell division requires the coordinated action of cell division proteins and murein (peptidoglycan) synthases. Interactions involving the essential cell division protein FtsN and murein synthases were studied by affinity chromatography with membrane fraction. The murein synthases PBP1A, PBP1B, and PBP3 had an affinity to immobilized FtsN. FtsN and PBP3, but not PBP1A, showed an affinity to immobilized PBP1B. The direct interaction between FtsN and PBP1B was confirmed by pulldown experiments and surface plasmon resonance. The interaction was also detected by bacterial two-hybrid analysis. FtsN and PBP1B could be cross-linked in intact cells of the wild type and in cells depleted of PBP3 or FtsW. FtsN stimulated the in vitro murein synthesis activities of PBP1B. Thus, FtsN could have a role in controlling or modulating the activity of PBP1B during cell division in Escherichia coli.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Muller, P.
Ewers, C.
Bertsche, U.
Anstett, M.
Kallis, T.
Breukink, E.
Fraipont, Claudine ;  Université de Liège - ULiège > Centre d'ingénierie des protéines
Terrak, Mohammed  ;  Université de Liège - ULiège > Centre d'ingénierie des protéines
Nguyen-Distèche, Martine ;  Université de Liège - ULiège > Centre d'ingénierie des protéines
Vollmer, W.
Language :
English
Title :
The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli
Publication date :
14 December 2007
Journal title :
Journal of Biological Chemistry
ISSN :
0021-9258
eISSN :
1083-351X
Publisher :
Amer Soc Biochemistry Molecular Biology Inc, Bethesda, United States - Maryland
Volume :
282
Issue :
50
Pages :
36394-36402
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
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