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Journal of Bacteriology, December 2001, p. 7190-7197, Vol. 183, No. 24
Department of Microbiology, Molecular
Genetics and Immunology, University of Kansas Medical Center, Kansas
City, Kansas 66160,1 and School of
Biological Sciences, University of Missouri
Received 22 May 2001/Accepted 21 September 2001
FtsZ, the ancestral homologue of eukaryotic tubulins, assembles
into the Z ring, which is required for cytokinesis in prokaryotic cells. Both FtsZ and tubulin have a GTPase activity associated with
polymerization. Interestingly, the ftsZ2 mutant is
viable, although the FtsZ2 mutant protein has dramatically reduced
GTPase activity due to a glycine-for-aspartic acid substitution within the synergy loop. In this study, we have examined the properties of
FtsZ2 and found that the reduced GTPase activity is not enhanced by
DEAE-dextran-induced assembly, indicating it has a defective catalytic
site. In the absence of DEAE-dextran, FtsZ2 fails to assemble unless
supplemented with wild-type FtsZ. FtsZ has to be at or above the
critical concentration for copolymerization to occur, indicating that
FtsZ is nucleating the copolymers. The copolymers formed are relatively
stable and appear to be stabilized by a GTP-cap. These results indicate
that FtsZ2 cannot nucleate assembly in vitro, although it must in vivo.
Furthermore, the stability of FtsZ-FtsZ2 copolymers argues that FtsZ2
polymers would be stable, suggesting that stable FtsZ polymers are able to support cell division.
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.24.7190-7197.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Assembly of an FtsZ Mutant Deficient in GTPase
Activity Has Implications for FtsZ Assembly and the Role of the Z
Ring in Cell Division
Kansas City, Kansas City,
Missouri 641102
*
Corresponding author. Mailing address: Department of
Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City, Kansas 66160. Phone (913) 588-7054. Fax:
(913) 588-7295. E-mail: jlutkenh{at}kumc.edu.
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