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Force Generation by a Dynamic Z-Ring in Escherichia Coli Cell Division
Jun F. Allard, Eric N. Cytrynbaum and J. Richard Mclntosh
Proceedings of the National Academy of Sciences of the United States of America
Vol. 106, No. 1 (Jan. 6, 2009), pp. 145-150
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/40272331
Page Count: 6
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
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FtsZ, a bacterial homologue of tubulin, plays a central role in bacterial cell division. It is the first of many proteins recruited to the division site to form the Z-ring, a dynamic structure that recycles on the time scale of seconds and is required for division to proceed. FtsZ has been recently shown to form rings inside tubular liposomes and to constrict the liposome membrane without the presence of other proteins, particularly molecular motors that appear to be absent from the bacterial proteome. Here, we propose a mathematical model for the dynamic turnover of the Z-ring and for its ability to generate a constriction force. Force generation is assumed to derive from GTP hydrolysis, which is known to induce curvature in FtsZ filaments. We find that this transition to a curved state is capable of generating a sufficient force to drive cell-wall invagination in vivo and can also explain the constriction seen in the in vitro liposome experiments. Our observations resolve the question of how FtsZ might accomplish cell division despite the highly dynamic nature of the Z-ring and the lack of molecular motors.
Proceedings of the National Academy of Sciences of the United States of America © 2009 National Academy of Sciences