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Description

Cell division protein FtsZ (UniProt: P17865, also known as Cell Division FtsZ GTPase, FtsZ) is encoded by the FtsZ (also known as BSU15290) gene (Gene ID: 935971) in Bacillus subtilis. FtsZ is homodimeric prokaryotic homologue of tubulin with GTPase activity. It is found in nearly all bacteria. It polymerizes in the presence of GTP to form higher-ordered polymers. It contains three GTP-binding sites that are located in the N-terminal region. The less conserved C-terminal domain contains residues that are important for GTP hydrolysis. FtsZ is shown to be essential for bacterial cell division and in association with FtzA (FtsAZ) it forms a contractile ring structure (Z ring) at the site of cell division. The regulation of the ring assembly controls the timing and the location of cell division. One of the major functions of FtsZ is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. The FtsZ treadmilling rate controls the rate of peptidoglycan synthesis and cell division. During bacterial cell division FtsZ co-localizes with SpoIIE, a dual function protein that contributes to the switch form medial to polar cell division during sporulation. The anti-FtsZ blot has also been used as control for sample loading (Ref.: Bisson-Filho, AW., et al., (2017). Science 355(6326), 739-743, Feucht, A., and Jeffery Errington, J (2005). Microbiology 151(6), 2053-2064, Lucet, I., et al. (2000). EMBO J. 19(7), 1467-1475, Lytvynenko, I., et al. (2019). Cell. 178(1), 76-90).