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Reconstitution of Contractile FtsZ Rings in Liposomes
Open accessAbstract
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.
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Cited by
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Loose, M., & Mitchison, T. J. (2014) · Nature Cell Biology · doi:10.1038/ncb2885 · Cited by 378
Octanol-assisted liposome assembly on chip
Deshpande, S., Caspi, Y., Meijering, A. E. C., & Dekker, C. (2016) · Nature Communications · doi:10.1038/ncomms10447 · Cited by 363
Structural basis for activation, assembly and membrane binding of ESCRT-III Snf7 filaments
Tang, S., Henne, W. M., Borbat, P. P., Buchkovich, N. J., Freed, J. H., Mao, Y., Fromme, J. C., & Emr, S. D. (2015) · eLife · doi:10.7554/elife.12548 · Cited by 156
Coordinating Bacterial Cell Division with Nutrient Availability: a Role for Glycolysis
Monahan, L. G., Hajduk, I. V., Blaber, S. P., Charles, I. G., & Harry, E. J. (2014) · mBio · doi:10.1128/mbio.00935-14 · Cited by 123
Divided we stand: splitting synthetic cells for their proliferation
Caspi, Y., & Dekker, C. (2014) · Systems and Synthetic Biology · doi:10.1007/s11693-014-9145-7 · Cited by 55
Metadata
- Authors
- Osawa, M., Anderson, D. E., & Erickson, H. P.
- Venue
- Science
- Published
- 2008-05-09
- Volume
- 320
- Issue
- 5877
- Pages
- 792-794
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2050339362
- Cited by
- 514
- References
- 0
- FWCI
- 15.64
- Type
- journal article
- Language
- en
- Open access
- green
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