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Ishikawa S., Kawai Y., Hiramatsu K., Kuwano M., and Ogasawara N. A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis. Mol Microbiol 60 (2006) 1364-1380
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This paper reports the crystal structure of one member of a family of division regulators present only in the actinomycetes. This information will provide valuable insight into the potential function and help suggest approaches to ask future questions.
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Xu Q., Traag B.A., Willemse J., McMullan D., Miller M.D., Elsliger M.A., Abdubek P., Astakhova T., Axelrod H.L., Bakolitsa C., et al. Structural and functional characterizations of SsgB, a conserved activator of developmental cell division in morphologically complex actinomycetes. J Biol Chem 284 (2009) 25268-25279. This paper reports the crystal structure of one member of a family of division regulators present only in the actinomycetes. This information will provide valuable insight into the potential function and help suggest approaches to ask future questions.
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Mosyak L., Zhang Y., Glasfeld E., Haney S., Stahl M., Seehra J., and Somers W.S. The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography. EMBO J 19 (2000) 3179-3191
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This paper shows that, if provided a membrane tether, FtsZ rings can be self-assembled and provide some constrictive force in the absence of another protein, opening a way to potentially reconstitute cytokinesis in vitro.
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Osawa M., Anderson D.E., and Erickson H.P. Reconstitution of contractile FtsZ rings in liposomes. Science 320 (2008) 792-794. This paper shows that, if provided a membrane tether, FtsZ rings can be self-assembled and provide some constrictive force in the absence of another protein, opening a way to potentially reconstitute cytokinesis in vitro.
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Erickson H.P. The FtsZ protofilament and attachment of ZipA - structural constraints on the FtsZ power stroke. Curr Opin Cell Biol 13 (2001) 55-60
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Gonzalez J.M., Velez M., Jimenez M., Alfonso C., Schuck P., Mingorance J., Vicente M., Minton A.P., and Rivas G. Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils. Proc Natl Acad Sci U S A 102 (2005) 1895-1900
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Erickson H.P. Modeling the physics of FtsZ assembly and force generation. Proc Natl Acad Sci U S A 106 (2009) 9238-9243
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Shen B., and Lutkenhaus J. The conserved C-terminal tail of FtsZ is required for the septal localization and division inhibitory activity of MinC(C)/MinD. Mol Microbiol 72 (2009) 410-424
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