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Super-resolution Imaging of the Bacterial Division Machinery
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Super-resolution Imaging of the Bacterial Division Machinery

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

Patrick Müller1, Carolin Ewers, Ute Bertsche

  • 1Microbial Genetics, University of Tübingen, 72076 Tübingen, Germany.

The Journal of Biological Chemistry
|October 17, 2007
PubMed

Insights

The essential bacterial cell division protein FtsN directly interacts with murein synthase PBP1B, suggesting FtsN modulates PBP1B activity during cell division in Escherichia coli.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Bacterial cell division is a complex process involving numerous proteins and enzymes.
  • Murein (peptidoglycan) synthases are crucial for cell wall formation during division.
  • The FtsN protein is essential for bacterial cytokinesis.

Purpose of the Study:

  • To investigate the interactions between the essential cell division protein FtsN and murein synthases.
  • To determine if FtsN directly interacts with and influences the activity of murein synthases.
  • To elucidate the role of FtsN in regulating murein synthesis during Escherichia coli cell division.

Main Methods:

  • Affinity chromatography using immobilized FtsN and PBP1B.
  • Pulldown experiments and surface plasmon resonance (SPR) to confirm direct interactions.
  • Bacterial two-hybrid analysis to detect protein-protein interactions in vivo.
  • In vitro murein synthesis assays to assess enzyme activity.

Main Results:

  • Murein synthases PBP1A, PBP1B, and PBP3 demonstrated affinity for immobilized FtsN.
  • FtsN and PBP3 showed affinity for immobilized PBP1B, with direct interaction confirmed by pulldown and SPR.
  • Bacterial two-hybrid analysis corroborated the FtsN-PBP1B interaction.
  • FtsN and PBP1B cross-linking occurred in intact cells, independent of PBP3 or FtsW.
  • FtsN significantly stimulated the in vitro murein synthesis activity of PBP1B.

Conclusions:

  • FtsN directly interacts with PBP1B, a key murein synthase.
  • This interaction is detectable both in vitro and in vivo.
  • FtsN appears to play a regulatory role in controlling or modulating PBP1B activity during bacterial cell division in Escherichia coli.

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