Abstract
FtsZ assembles in vitro into protofilaments (pfs) that are one subunit thick and ~50 subunits long. In vivo these pfs assemble further into the Z ring, which, along with accessory division proteins, constricts to divide the cell. We have reconstituted Z rings in liposomes in vitro, using pure FtsZ that was modified with a membrane targeting sequence to directly bind the membrane. This FtsZ-mts assembled Z rings and constricted the liposomes without any accessory proteins. We proposed that the force for constriction was generated by a conformational change from straight to curved pfs. Evidence supporting this mechanism came from switching the membrane tether to the opposite side of the pf. These switched-tether pfs assembled “inside-out” Z rings, and squeezed the liposomes from the outside, as expected for the bending model. We propose three steps for the full process of cytokinesis: (a) pf bending generates a constriction force on the inner membrane, but the rigid peptidoglycan wall initially prevents any invagination; (b) downstream proteins associate to the Z ring and remodel the peptidoglycan, permitting it to follow the constricting FtsZ to a diameter of ~250 nm; the final steps of closure of the septum and membrane fusion are achieved by excess membrane synthesis and membrane fluctuations.
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Notes
- 1.
This study quantitates the number of molecules of almost all proteins in E. coli MG1655, under three growth conditions. Our Table 5.1 collects their data for cell division and cytoskeletal proteins.
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Erickson, H.P., Osawa, M. (2017). FtsZ Constriction Force – Curved Protofilaments Bending Membranes. In: Löwe, J., Amos, L. (eds) Prokaryotic Cytoskeletons. Subcellular Biochemistry, vol 84. Springer, Cham. https://doi.org/10.1007/978-3-319-53047-5_5
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