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Filamenting temperature-sensitive mutant Z protein (FtsZ) is a prokaryotic homologue of eukaryotic tubulin that plays an essential role in bacterial cell division. It assembles into a dynamic ring structure called the Z ring at the future site of septation, marking where the bacterium will divide into two daughter cells. The formation and constriction of this ring are critical steps in binary fission. FtsZ exhibits GTPase activity and polymerizes head-to-tail to form protofilaments that make up the contractile scaffold required for cytokinesis. It recruits additional proteins involved in septum formation and membrane invagination. FtsZ is found almost universally among bacteria, many archaea, chloroplasts, and some mitochondria. Its structural similarity to tubulin—despite low sequence identity—highlights its evolutionary importance as part of an ancient cytoskeletal family involved in fundamental cellular processes across all domains of life. Due to its essential function exclusively within prokaryotes (and organelles derived from them), FtsZ has emerged as an attractive target for novel antibacterial therapies aimed at disrupting bacterial replication without affecting human cells.
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