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Slow polymerization of Mycobacterium tuberculosis FtsZ
E L White1, L J Ross, R C Reynolds
1Drug Discovery Division, Southern Research Institute, Birmingham, AL 35205, USA. white@sri.org
Journal of Bacteriology
|June 27, 2000
Summary
Mycobacterium tuberculosis FtsZ, a cell division protein, exhibits slow polymerization and depolymerization. A tubulin inhibitor, SRI 7614, effectively blocks its polymerization and GTPase activity.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- FtsZ is a crucial protein for bacterial cell division.
- Understanding FtsZ from Mycobacterium tuberculosis (Mtb) is vital for developing new tuberculosis treatments.
Purpose of the Study:
- To characterize the polymerization properties of Mtb FtsZ.
- To investigate the effects of a novel tubulin polymerization inhibitor on Mtb FtsZ.
Main Methods:
- Expression and purification of recombinant Mtb FtsZ in E. coli.
- GTPase activity assays.
- Light scattering and electron microscopy to study polymerization.
- Inhibition assays using SRI 7614.
Main Results:
- Recombinant Mtb FtsZ displays GTPase activity and polymerizes in a manner similar to other FtsZs, but with slower kinetics.
- Polymerization requires Mg(2+) and GTP, with a minimum concentration of 3 microM.
- Electron microscopy revealed ordered aggregates of protofilaments in polymerized Mtb FtsZ.
- SRI 7614 inhibited Mtb FtsZ polymerization, GTP hydrolysis, and reduced polymer formation.
Conclusions:
- Mtb FtsZ polymerization is a slow process compared to E. coli FtsZ.
- The tubulin inhibitor SRI 7614 demonstrates potential as an inhibitor of Mtb FtsZ, offering a possible therapeutic strategy against tuberculosis.