FtsZ

FtsZ is a protein encoded by the ftsZ gene that assembles into a ring at the future site of the septum of bacterial cell division. This is a prokaryotic homologue to the eukaryotic protein tubulin. FtsZ has been named after "Filamenting temperature-sensitive mutant Z". The hypothesis was that cell division mutants of E. coli would grow as filaments due to the inability of the daughter cells to separate from one another.

Discovery of the bacterial cytoskeleton is fairly recent. FtsZ was the first protein of the prokaryotic cytoskeleton to be identified.

The gene was discovered in the 1950s by Y. Hirota () and his colleagues in a screen for bacterial cell division mutants. In 1991 it was shown by Erfei Bi and Joseph Lutkenhaus that FtsZ assembled into the Z-ring.

Nuclear-encoded FtsZ in the moss Physcomitrella patens is required for chloroplast division and was the first identified protein essential for organelle division.

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. In liposomes Osawa (2009) showed FtsZ is capable of exerting a contractile force with no other proteins present.

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