title: Analyses of mechanisms for force generation during cell septation in Escherichia coli.
abstract: Escherichia coli is a rod-shaped bacterium that divides at its midplane, partitioning its cellular material into two roughly equal parts. At the appropriate time, a septum forms, creating the two daughter cells. Septum formation starts with the appearance of a ring of FtsZ proteins on the cell membrane at midplane. This Z-ring causes an invagination in the membrane, which is followed by growth of two new endcaps for the daughter cells. Invagination occurs against a cell overpressure of several atmospheres. A model is presented for the shape of the cell as determined by the tension in the Z-ring. This model allows the calculation of the force required for invagination. Then three possible models to generate the force necessary to achieve invagination are presented and analyzed. These models are based on converting GTP-bound FtsZ polymeric structures to GDP-bound FtsZ structures, which then leave the polymer. Each model is able to generate the force by relating the hydrolyzation to an irreversible molecular binding event, resulting in a net motion of putative anchors for the structures. All three models show that cross-linking the FtsZ protofilaments into a polymer structure allows the removal of GDP-FtsZ without interrupting the structure during force generation, as would happen for a simple polymeric chain.
authors.affiliation: Department of Mathematical Sciences, Rensselaer Polytechnic Institute, Troy, NY 12180-3590, USA. drewd@rpi.edu
authors.forename: Donald A
authors.initials: DA
authors.lastname: Drew
authors.forename: Gretchen A
authors.initials: GA
authors.lastname: Koch
authors.forename: Heather
authors.initials: H
authors.lastname: Vellante
authors.forename: Ronak
authors.initials: R
authors.lastname: Talati
authors.forename: Oswaldo
authors.initials: O
authors.lastname: Sanchez
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism; D002455:Cell Division / Q000502:physiology; D002462:Cell Membrane / Q000502:physiology; D003598:Cytoskeletal Proteins / Q000378:metabolism; D004926:Escherichia coli / Q000166:cytology* / Q000378:metabolism; D006153:Guanosine Diphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D008954:Models, Biological; D009716:Numerical Analysis, Computer-Assisted
chemical_list: D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate