The bacterial cell division proteins ftsA and ftsZ self-organize into dynamic cytoskeletal patterns Journal Article


Author(s): Loose, Martin; Mitchison, Timothy J
Article Title: The bacterial cell division proteins ftsA and ftsZ self-organize into dynamic cytoskeletal patterns
Affiliation
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.
Keywords: unclassified drug; Bacteria (microorganisms)bacterial protein; FtsA protein; FtsZ protein
Journal Title: Nature Cell Biology
Volume: 16
Issue 1
ISSN: 1476-4679
Publisher: Nature Publishing Group  
Date Published: 2014-01-01
Start Page: 38
End Page: 46
Sponsor: M.L. is supported by fellowships from EMBO (ALTF 394-2011) and HFSP (LT000466/2012). Cytoskeleton dynamics research in the T.J.M. group is supported by NIH-GM39565.
DOI: 10.1038/ncb2885
Open access: no