The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli

Patrick Müller; C. Ewers; U. Bertsche; M. Anstett; T. Kallis; E.J. Breukink; Claudine Fraipont; Mohammed Terrak; Martine Nguyen-Distèche; W. Vollmer

The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli

Patrick Müller, C. Ewers, U. Bertsche, M. Anstett, T. Kallis, E.J. Breukink, Claudine Fraipont, Mohammed Terrak, Martine Nguyen-Distèche, W. Vollmer

Dept of Chemistry

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

Abstract

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.

Original language	Undefined/Unknown
Pages (from-to)	36394-36402
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	282
Issue number	50
Publication status	Published - 2007

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@article{54e4211ebd3e41afa9c40878d0b7d1de,

title = "The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli",

abstract = "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.",

author = "Patrick M{\"u}ller and C. Ewers and U. Bertsche and M. Anstett and T. Kallis and E.J. Breukink and Claudine Fraipont and Mohammed Terrak and Martine Nguyen-Dist{\`e}che and W. Vollmer",

year = "2007",

language = "Undefined/Unknown",

volume = "282",

pages = "36394--36402",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "50",

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TY - JOUR

T1 - The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli

AU - Müller, Patrick

AU - Ewers, C.

AU - Bertsche, U.

AU - Anstett, M.

AU - Kallis, T.

AU - Breukink, E.J.

AU - Fraipont, Claudine

AU - Terrak, Mohammed

AU - Nguyen-Distèche, Martine

AU - Vollmer, W.

PY - 2007

Y1 - 2007

N2 - 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.

AB - 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.

M3 - Article

SN - 0021-9258

VL - 282

SP - 36394

EP - 36402

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 50

ER -