The bacterial cell division proteins ftsA and ftsZ self-organize into dynamic cytoskeletal patterns Loose, Martin ; https://orcid.org/0000-0001-7309-9724 Mitchison, Timothy Bacterial cytokinesis is commonly initiated by the Z-ring, a cytoskeletal structure that assembles at the site of division. Its primary component is FtsZ, a tubulin superfamily GTPase, which is recruited to the membrane by the actin-related protein FtsA. Both proteins are required for the formation of the Z-ring, but if and how they influence each other's assembly dynamics is not known. Here, we reconstituted FtsA-dependent recruitment of FtsZ polymers to supported membranes, where both proteins self-organize into complex patterns, such as fast-moving filament bundles and chirally rotating rings. Using fluorescence microscopy and biochemical perturbations, we found that these large-scale rearrangements of FtsZ emerge from its polymerization dynamics and a dual, antagonistic role of FtsA: recruitment of FtsZ filaments to the membrane and negative regulation of FtsZ organization. Our findings provide a model for the initial steps of bacterial cell division and illustrate how dynamic polymers can self-organize into large-scale structures. Nature Publishing Group 2014 info:eu-repo/semantics/article doc-type:article text http://purl.org/coar/resource_type/c_2df8fbb1 https://research-explorer.ista.ac.at/record/1990 Loose M, Mitchison T. The bacterial cell division proteins ftsA and ftsZ self-organize into dynamic cytoskeletal patterns. <i>Nature Cell Biology</i>. 2014;16:38-46. doi:<a href="https://doi.org/10.1038/ncb2885">10.1038/ncb2885</a> eng info:eu-repo/semantics/altIdentifier/doi/10.1038/ncb2885 info:eu-repo/semantics/altIdentifier/pmid/24316672 info:eu-repo/semantics/closedAccess