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Structural basis for the geometry-driven localization of a small protein.

Richard L Gill1, Jean-Philippe Castaing2, Jen Hsin3

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Bacterial protein SpoVM senses membrane curvature by inserting its helix into lipid acyl chains. This mechanism drives its localization to convex forespore membranes during Bacillus subtilis sporulation.

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Area of Science:

  • Microbiology
  • Biophysics
  • Structural Biology

Background:

  • Bacteria utilize shape-sensing proteins to localize to specific membrane curvatures.
  • During Bacillus subtilis sporulation, the forespore is the sole convex membrane compartment.
  • SpoVM protein is known to localize to the forespore.

Purpose of the Study:

  • To elucidate the molecular mechanism by which SpoVM senses and localizes to convex membranes.
  • To investigate the role of SpoVM's amphipathic helix in membrane interaction and curvature sensing.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy of SpoVM and a localization mutant (SpoVM(P9A)).
  • Molecular dynamics (MD) simulations to model SpoVM-membrane interactions.
  • Binding assays using spherical supported lipid bilayers.
  • Monte Carlo simulations to analyze localization behavior.

Main Results:

  • SpoVM's amphipathic alpha-helix inserts deeply into the lipid bilayer.
  • Extensive interactions between SpoVM and acyl chains were observed, indicating sensing of packing differences.
  • SpoVM preferentially binds to slightly convex membranes, distinct from high-curvature sensors.
  • Cooperative interactions between SpoVM molecules may enhance localization.

Conclusions:

  • SpoVM employs a unique mechanism of deep membrane insertion and acyl chain interaction for curvature sensing.
  • This mechanism drives SpoVM's preferential localization to the convex forespore membrane.
  • The findings suggest a conserved mechanism for organelle protein localization across different cellular systems.