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Originally published in Science Express on 17 April 2008
Science 9 May 2008:
Vol. 320. no. 5877, pp. 792 - 794
DOI: 10.1126/science.1154520
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Reports

Reconstitution of Contractile FtsZ Rings in Liposomes

Masaki Osawa, David E. Anderson, Harold P. Erickson*

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.

Department of Cell Biology, Duke University Medical Center, Durham, NC 27710–3709, USA.

* To whom correspondence should be addressed. E-mail: h.erickson{at}cellbio.duke.edu

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