FtsZ was the first protein of the prokaryotic cytoskeleton to be identified. During cell division, FtsZ is the first protein to move to the division site, and is essential for recruiting other proteins that produce a new cell wall between the dividing cells. FtsZ's role in cell division is analogous to that of actin in eukaryotic cell division, but unlike the actin-myosin ring in eukaryotes, FtsZ has no known motor protein associated with it. The origin of the cytokinetic force thus remains unclear, but it is believed that the localized synthesis of new cell wall produces at least part of this force. It is interesting to note that L-form bacteria that lack a cell wall do not require FtsZ for division, which implies that bacteria may have retained components of an ancestral mode of cell division.
Much is known about the dynamic polymerization activities of tubulin and microtubules, but little is known about these activities in FtsZ. While it is known that single-stranded tubulin protofilaments form into 13 stranded microtubules, the multistranded structure of the FtsZ-containing Z-ring is not known. It is only speculated that the structure consists of overlapping protofilaments. Recently, proteins similar to tubulin and FtsZ have been discovered in large plasmids found in Bacillus species. They are believed to function as components of segrosomes, which are multiprotein complexes that partition chromosomes/plasmids in bacteria. The plasmid homologs of tubulin/FtsZ seem to have conserved the ability to polymerize into filaments.