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Reconstitution of contractile FtsZ rings in liposomes.

FtsZ is a tubulin homolog and the major cytoskeletal protein in bacterial cell division. It assembles into the Z ring, which contains FtsZ and a dozen other division proteins, and constricts to divide the cell. We have constructed a membrane-targeted FtsZ (FtsZ-mts) by splicing an amphipathic helix to its C terminus. When mixed with lipid vesicles, FtsZ-mts was incorporated into the interior of some tubular vesicles. There it formed multiple Z rings that could move laterally in both directions along the length of the liposome and coalesce into brighter Z rings. Brighter Z rings produced visible constrictions in the liposome, suggesting that FtsZ itself can assemble the Z ring and generate a force. No other proteins were needed for assembly and force generation.

Pubmed ID: 18420899

Authors

  • Osawa M
  • Anderson DE
  • Erickson HP

Journal

Science (New York, N.Y.)

Publication Data

May 9, 2008

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM66014
  • Agency: NIGMS NIH HHS, Id: R01 GM066014
  • Agency: NIGMS NIH HHS, Id: R01 GM066014-01

Mesh Terms

  • Bacterial Proteins
  • Cell Membrane
  • Cytoskeletal Proteins
  • Escherichia coli
  • Escherichia coli Proteins
  • Liposomes
  • Membrane Proteins
  • Protein Binding
  • Protein Transport
  • Recombinant Proteins