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FtsZ condensates: an in vitro electron microscopy study.

David Popp1, Mitsusada Iwasa, Akihiro Narita

  • 1ERATO Actin Filament Dynamics Project, Japan Science and Technology Corporation, c/o RIKEN Harima Institute at Spring 8, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan. dpopp@spring8.or.jp

Biopolymers
|January 13, 2009
PubMed
Summary
This summary is machine-generated.

Molecular crowding drives the formation of bacterial cell division protein FtsZ into complex structures like rings and helices in vitro. These findings illuminate the in vivo assembly of FtsZ during cell division.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Microbiology

Background:

  • The bacterial cell division protein FtsZ forms dynamic rings and spirals in vivo, observed previously only via low-resolution microscopy.
  • Understanding FtsZ suprastructure formation is crucial for comprehending prokaryotic cell division.

Purpose of the Study:

  • To investigate the in vitro assembly of FtsZ supramolecular structures under conditions mimicking the crowded prokaryotic cellular environment.
  • To elucidate the role of molecular crowding in FtsZ polymerization and higher-order structure formation.

Main Methods:

  • In vitro assembly of FtsZ protofilaments in dilute buffer and in the presence of crowding agents.
  • High-resolution electron microscopy to characterize the morphology and molecular arrangement of FtsZ suprastructures.
  • Varying crowding agent concentrations to determine critical assembly thresholds.

Main Results:

  • FtsZ assembles into single protofilaments in dilute solutions but forms polymorphic structures (rings, toroids, helices, bundles) above a critical crowding concentration.
  • Observed helical structures resemble in vivo FtsZ arrangements, while rings and toroids may represent novel energy-minimized states.
  • Electron microscopy revealed detailed molecular arrangements within these complex FtsZ assemblies.

Conclusions:

  • Molecular crowding is a key factor in the in vivo formation of FtsZ rings and spirals by enhancing inter-protofilament interactions.
  • The study presents novel FtsZ supramolecular structures (rings, toroids) formed under crowding conditions, potentially reflecting late-stage Z-ring constriction.
  • High-resolution microscopy provides insights into the molecular basis of FtsZ assembly and its role in bacterial cytokinesis.