title: Force generation in bacteria without nucleotide-dependent bending of cytoskeletal filaments.
abstract: Binary cell division in bacteria occurs via the formation and subsequent contraction of a polymeric ring, the so-called Z ring, at the middle of the cell. This ring is made of filamenting temperature-sensitive Z (FtsZ) proteins and it shrinks in radius to generate a contractile radial force on the cell membrane. Although a few models have been proposed, the ring contraction mechanism still remains a mystery. The models rely on various physical properties of the FtsZ filaments, some of which have been verified through in vitro experiments and some of which remain unclear. A feature common to all these models is the hydrolysis-driven transition of FtsZ filaments from straight to curved conformations. While the intrinsic curvature of FtsZ filaments has been experimentally established beyond doubt, evidence has been mounting against the existence of any transition between the straight FtsZ-GTP and the curved FtsZ-GDP conformations. Preliminary results from our earlier work [B. Ghosh and A. Sain, Phys. Rev. Lett. 101, 178101 (2008)] indicated that hydrolysis-induced bending is not necessary for Z-ring contraction. Since then many new experimental observations have been reported on this subject and in view of these here we argue that our model appears even more plausible than before. In addition, we have explored more realistic features, such as how the length distribution of FtsZ filaments in the cytoplasm may influence the contraction dynamics, and we have also demonstrated that the Z ring retains approximately the same number of monomers, although not the same monomers, during the course of contraction as reported by fluorescence experiments.
authors: Department of Physics, Indian Institute of Technology-Bombay, Powai, Mumbai, India.
authors: Biplab
authors: B
authors: Ghosh
authors: Anirban
authors: A
authors: Sain
mesh_terms: D001419:Bacteria / Q000166:cytology* / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000737:chemistry / Q000378:metabolism; D003599:Cytoskeleton / Q000737:chemistry* / Q000378:metabolism*; D006153:Guanosine Diphosphate / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism*; D006868:Hydrolysis; D008958:Models, Molecular; D009010:Monte Carlo Method; D017434:Protein Structure, Tertiary
chemical_list: D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate