Journal
ANNUAL REVIEW OF BIOPHYSICS, VOL 49, 2020
Volume 49, Issue -, Pages 309-341Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biophys-121219-081703
Keywords
FtsZ; bacterial cell division; cell wall constriction; cytoskeleton dynamics; septum synthesis; single-molecule imaging
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Funding
- National Institutes of Health (NIH) [T32 GM008403]
- NIH [R01GM086447, GM125656]
- Hamilton Smith Innovative Research Award
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The FtsZ protein is a highly conserved bacterial tubulin homolog. In vivo, the functional form of FtsZ is the polymeric, ring-like structure (Z-ring) assembled at the future division site during cell division. While it is clear that the Z-ring plays an essential role in orchestrating cytokinesis, precisely what its functions are and how these functions are achieved remain elusive. In this article, we review what we have learned during the past decade about the Z-ring's structure, function, and dynamics, with a particular focus on insights generated by recent high-resolution imaging and single-molecule analyses. We suggest that the major function of the Z-ring is to govern nascent cell pole morphogenesis by directing the spatiotemporal distribution of septal cell wall remodeling enzymes through the Z-ring's GTP hydrolysis-dependent treadmilling dynamics. In this role, FtsZ functions in cell division as the counterpart of the cell shape-determining actin homolog MreB in cell elongation.
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