Independence between GTPase active sites in the Escherichia coli cell division protein FtsZ.
| Autor: | Salvarelli E; Servicio de Microbiología, Hospital Universitario La Paz, IdiPAZ, Madrid, Spain., Krupka M, Rivas G, Vicente M, Mingorance J |
|---|---|
| Jazyk: | angličtina |
| Zdroj: | FEBS letters [FEBS Lett] 2011 Dec 15; Vol. 585 (24), pp. 3880-3. Date of Electronic Publication: 2011 Nov 03. |
| DOI: | 10.1016/j.febslet.2011.10.046 |
| Abstrakt: | 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. (Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.) |
| Databáze: | MEDLINE |
| Externí odkaz: |
|
Plný text