---
res:
  bibo_abstract:
  - '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.@eng'
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Martin
      foaf_name: Loose, Martin
      foaf_surname: Loose
      foaf_workInfoHomepage: http://www.librecat.org/personId=462D4284-F248-11E8-B48F-1D18A9856A87
    orcid: 0000-0001-7309-9724
  - foaf_Person:
      foaf_givenName: Timothy
      foaf_name: Mitchison, Timothy
      foaf_surname: Mitchison
  bibo_doi: 10.1038/ncb2885
  bibo_volume: 16
  dct_date: 2014^xs_gYear
  dct_language: eng
  dct_publisher: Nature Publishing Group@
  dct_title: The bacterial cell division proteins ftsA and ftsZ self-organize into
    dynamic cytoskeletal patterns@
  fabio_hasPubmedId: '24316672'
...