Force generation by a dynamic Z-ring in Escherichia coli cell division.
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.
Allard
Jun F
JF
Department of Mathematics, University of British Columbia, Vancouver, BC, Canada V6T 1Z2.
Cytrynbaum
Eric N
EN
D001426:Bacterial Proteins / Q000502:physiology*; D001696:Biomechanical Phenomena; D002455:Cell Division; D003598:Cytoskeletal Proteins / Q000502:physiology*; D004926:Escherichia coli / Q000166:cytology*; D029968:Escherichia coli Proteins / Q000502:physiology; D006160:Guanosine Triphosphate / Q000378:metabolism; D008081:Liposomes; D008954:Models, Biological
D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; D029968:Escherichia coli Proteins; C071525:FtsZ protein, Bacteria; D008081:Liposomes; D006160:Guanosine Triphosphate