Reconstitution of contractile FtsZ rings in liposomes
Reconstitution of contractile FtsZ rings in liposomes
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DOI:
10.1126/science.1154520
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发表时间:
2008-05-09
期刊:
影响因子:
56.9
通讯作者:
Erickson, Harold P.
中科院分区:
文献类型:
--
作者:
Osawa, Masaki;Anderson, David E.;Erickson, Harold P.
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.