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Originally published In Press as doi:10.1074/jbc.M206723200 on September 4, 2002

J. Biol. Chem., Vol. 277, Issue 45, 43262-43270, November 8, 2002
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Reversible Unfolding of FtsZ Cell Division Proteins from Archaea and Bacteria
COMPARISON WITH EUKARYOTIC TUBULIN FOLDING AND ASSEMBLY*

José Manuel AndreuDagger §, María Angela OlivaDagger , and Octavio Monasterio

From the Dagger  Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Velázquez 144, 28006 Madrid, Spain and the  Departamento de Biología, Facultad de Ciencias, Universidad de Chile, Casilla 653, Santiago, Chile

The stability, refolding, and assembly properties of FtsZ cell division proteins from Methanococcus jannaschii and Escherichia coli have been investigated. Their guanidinium chloride unfolding has been studied by circular dichroism spectroscopy. FtsZ from E. coli and tubulin released the bound guanine nucleotide, coinciding with an initial unfolding stage at low denaturant concentrations, followed by unfolding of the apoprotein. FtsZ from M. jannaschii released its nucleotide without any detectable secondary structural change. It unfolded in an apparently two-state transition at larger denaturant concentrations. Isolated FtsZ polypeptide chains were capable of spontaneous refolding and GTP-dependent assembly. The homologous eukaryotic tubulin monomers misfold in solution, but fold within the cytosolic chaperonin CCT. Analysis of the extensive tubulin loop insertions in the FtsZ/tubulin common core and of the intermolecular contacts in model microtubules and tubulin-CCT complexes shows a loop insertion present at every element of lateral protofilament contact and at every contact of tubulin with CCT (except at loop T7). The polymers formed by purified FtsZ have a distinct limited protofilament association in comparison with microtubules. We propose that the loop insertions of tubulin and its CCT-assisted folding coevolved with the lateral association interfaces responsible for extended two-dimensional polymerization into microtubule polymers.

* This work was supported in part by MCyT Grant BIO99-0859-C03-02/BIO2000-0748, the Programa de Grupos Estratégicos de la Comunidad de Madrid (to J. M. A.), an FPI predoctoral fellowship (to M. A. O.), and FONDECYT Grant 1010848 (to O. M.).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 should be addressed. Tel.: 34-91-561-1800 (ext. 4380); Fax: 34-91-562-7518; E-mail: j.m.andreu@cib.csic.es.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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