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Journal of Bacteriology, July 2000, p. 4028-4034, Vol. 182, No. 14
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Slow Polymerization of Mycobacterium tuberculosis FtsZ

E. Lucile White,* Larry J. Ross, Robert C. Reynolds, Lainne E. Seitz, Georgia D. Moore, and David W. Borhani

Drug Discovery Division, Southern Research Institute, Birmingham, Alabama

Received 17 February 2000/Accepted 25 April 2000

The essential cell division protein, FtsZ, from Mycobacterium tuberculosis has been expressed in Escherichia coli and purified. The recombinant protein has GTPase activity typical of tubulin and other FtsZs. FtsZ polymerization was studied using 90° light scattering. The mycobacterial protein reaches maximum polymerization much more slowly (~10 min) than E. coli FtsZ. Depolymerization also occurs slowly, taking 1 h or longer under most conditions. Polymerization requires both Mg2+ and GTP. The minimum concentration of FtsZ needed for polymerization is 3 µM. Electron microscopy shows that polymerized M. tuberculosis FtsZ consists of strands that associate to form ordered aggregates of parallel protofilaments. Ethyl 6-amino-2,3-dihydro-4-phenyl-1H-pyrido[4,3-b][1,4]diazepin-8-ylcarbamate (SRI 7614), an inhibitor of tubulin polymerization synthesized at Southern Research Institute, inhibits M. tuberculosis FtsZ polymerization, inhibits GTP hydrolysis, and reduces the number and sizes of FtsZ polymers.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, Southern Research Institute, 2000 Ninth Ave. South, Birmingham, AL 35205. Phone: (205) 581-2344. Fax: (205) 581-2877. E-mail: white{at}sri.org.

Journal of Bacteriology, July 2000, p. 4028-4034, Vol. 182, No. 14
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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