FtsZ is required for the formation of a ring structure, known as the Z ring, at the site of cell or organelle division. Contraction of the Z ring leads to fission of the cell or organelle.
The FtsZ family of proteins is widely conserved among prokaryotes and plants where it is used in chloroplast division. However, FtsZ is notably absent in a branch of the archaea, several branches of bacteria and in the mitochondria of most eukaryotes.
FtsZ is a structural homologue of tubulin, and its biochemical properties also resemble those of tubulins, including its ability to bind and hydrolyse GTP and assemble into protofilaments. Unlike tubulin, however, FtsZ does not form microtubules, and the precise nature of FtsZ-containing macromolecules in vivo is not known.
The Z ring localizes to the centre of Escherichia coli cells at the correct time during the cell cycle. There has been much progress in understanding how two negative regulatory systems ensure the proper spatial regulation of the Z ring. Several regulators of Z-ring assembly have been discovered that might interact with the spatial and temporal regulatory network.
Whereas the requirement of FtsZ in cytokinesis is well-established, it is unclear whether the Z ring drives cytokinesis actively by mechanical pulling against the membrane or more passively by the recruitment of cell-wall-synthesis enzymes, or both. Recent evidence indicates that a significant proportion of the FtsZ protein population is not ring associated, and that these proteins might have additional functions besides cytokinesis, such as the maintenance of cell shape.
Good progress has been made in understanding the important role of FtsZ in the fission of organelles, particularly in chloroplasts. FtsZ proteins work along with dynamin and other components to divide organelles.
Binary fission of many prokaryotes as well as some eukaryotic organelles depends on the FtsZ protein, which self-assembles into a membrane-associated ring structure early in the division process. FtsZ is homologous to tubulin, the building block of the microtubule cytoskeleton in eukaryotes. Recent advances in genomics and cell-imaging techniques have paved the way for the remarkable progress in our understanding of fission in bacteria and organelles.
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Work in the Margolin laboratory is supported by grants from the National Institutes of Health and the National Science Foundation. I thank H. Erickson for helpful advice. I apologize to colleagues whose work was not cited here because of space limitations.
The author declares no competing financial interests.
Pertaining to the group of archaea that includes the methanogens and extreme halophiles.
The group of archaea that includes the extreme thermophiles.
The organized form of a bacterial chromosome.
Describing the engulfment of one cell by another larger cell, with the engulfed cell evolving into an organelle.
- COOPERATIVE ASSEMBLY
The affinity of subunits for a polymer increases as more subunits are assembled, displaying a critical concentration below which little assembly occurs.
- ISODESMIC ASSEMBLY
The opposite of cooperative assembly, in that the affinity of each new subunit for a polymer is independent of the subunit concentration.
- MIN SYSTEM
A group of two or three bacterial proteins that inhibit unwanted formation of the Z ring at the cell poles.
The DNA-replication protein machinery.
- SOS RESPONSE
Inducible DNA repair system in bacteria invoked in response to a sudden increase in DNA damage.
Describes an integral membrane protein that has one cytoplasmic, transmembrane and periplasmic domain.
(Fluorescence recovery after photobleaching). A microscopic technique used to measure the movement (for example, diffusion rates) of fluorescently tagged molecules over time in vivo. Specific regions in a cell are irreversibly photobleached using a laser; fluorescence is restored by diffusion of fluorescently tagged unbleached molecules into the bleached area.
A family of GTPases that are important for membrane scission.
- STROMAL COMPARTMENT
The inner compartment of the chloroplast.
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Margolin, W. FtsZ and the division of prokaryotic cells and organelles. Nat Rev Mol Cell Biol 6, 862–871 (2005). https://doi.org/10.1038/nrm1745
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