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J. Biol. Chem., Vol. 276, Issue 15, 11743-11753, April 13, 2001
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From the FtsZ is a bacterial homolog of tubulin that is
essential for prokaryotic cytokinesis. In vitro, GTP
induces FtsZ to assemble into straight, 5-nm-wide polymers. Here we
show that the polymerization of these FtsZ filaments most closely
resembles noncooperative (or "isodesmic") assembly; the polymers
are single-stranded and assemble with no evidence of a nucleation phase
and without a critical concentration. We have developed a model for the
isodesmic polymerization that includes GTP hydrolysis in the scheme.
The model can account for the lengths of the FtsZ polymers and their maximum steady state nucleotide hydrolysis rates. It predicts that
unlike microtubules, FtsZ protofilaments consist of GTP-bound FtsZ
subunits that hydrolyze their nucleotide only slowly and are connected
by high affinity longitudinal bonds with a nanomolar KD.
Polymerization of FtsZ, a Bacterial Homolog of Tubulin
IS ASSEMBLY COOPERATIVE?*
§,
Department of Cell Biology, Duke University
Medical Center, Durham, North Carolina 27710 and ¶ Biology
Department, Brookhaven National Laboratory,
Upton, New York 11973
*
This work was supported in part by National Institutes of
Health Grant GM28553.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence may be addressed. E-mail:
H.Erickson@cellbio.duke.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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