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Updated: May 27, 2026

FtsZ Polymerization Assays: Simple Protocols and Considerations
Published on: November 16, 2013
Independence between GTPase active sites in the Escherichia coli cell division protein FtsZ
Estefanía Salvarelli1, Marcin Krupka, Germán Rivas
1Servicio de Microbiología, Hospital Universitario La Paz, IdiPAZ, Madrid, Spain.
Abstract:
We have analyzed the substrate kinetics of the GTPase activity of FtsZ and the effects of two different GTPase inhibitors, GDP and the slowly hydrolyzable GTP analogue GMPCPP. In the absence of inhibitors the GTPase activity follows simple Michaelis-Menten kinetics, and both GDP and GMPCPP inhibited the activity in a competitive manner. These results indicate that the GTPase active sites in FtsZ filaments are independent of each other, a feature relevant to elucidate the role of GTP hydrolysis in FtsZ function and cell division.
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