Force generation by a dynamic Z-ring in Escherichia coli cell division
- 6 January 2009
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 106 (1), 145-150
- https://doi.org/10.1073/pnas.0808657106
Abstract
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.Keywords
This publication has 38 references indexed in Scilit:
- Polymerization and Bundling Kinetics of FtsZ FilamentsBiophysical Journal, 2008
- Allosteric Models for Cooperative Polymerization of Linear PolymersBiophysical Journal, 2008
- Kinetic Modeling of the Assembly, Dynamic Steady State, and Contraction of the FtsZ Ring in Prokaryotic CytokinesisPLoS Computational Biology, 2008
- FtsZ Bacterial Cytoskeletal Polymers on Curved Surfaces: The Importance of Lateral InteractionsBiophysical Journal, 2008
- Reconstitution of Contractile FtsZ Rings in LiposomesScience, 2008
- Energetics and Geometry of FtsZ Polymers: Nucleated Self-Assembly of Single ProtofilamentsBiophysical Journal, 2008
- The structure of FtsZ filaments in vivo suggests a force-generating role in cell divisionThe EMBO Journal, 2007
- Z-ring force and cell shape during division in rod-like bacteriaProceedings of the National Academy of Sciences, 2007
- A Mechanical Explanation for Cytoskeletal Rings and Helices in BacteriaBiophysical Journal, 2007
- SlmA, a Nucleoid-Associated, FtsZ Binding Protein Required for Blocking Septal Ring Assembly over Chromosomes in E. coliMolecular Cell, 2005