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Originally published In Press as doi:10.1074/jbc.M301640200 on March 12, 2003

J. Biol. Chem., Vol. 278, Issue 20, 18015-18021, May 16, 2003
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Analysis of the Interaction of Small Heat Shock Proteins with Unfolding Proteins*

Thusnelda Stromer, Monika EhrnspergerDagger , Matthias Gaestel§, and Johannes Buchner

From the Institut für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany and § Medizinische Hochschule Hannover, Inst. für Biochemie, Carl-Neuberg-Str. 1, D-30625 Hannover, Germany

The ubiquitous small heat shock proteins (sHsps) are efficient molecular chaperones that interact with nonnative proteins, prevent their aggregation, and support subsequent refolding. No obvious substrate specificity has been detected so far. A striking feature of sHsps is that they form large complexes with nonnative proteins. Here, we used several well established model chaperone substrates, including citrate synthase, alpha -glucosidase, rhodanese, and insulin, and analyzed their interaction with murine Hsp25 and yeast Hsp26 upon thermal unfolding. The two sHsps differ in their modes of activation. In contrast to Hsp25, Hsp26 undergoes a temperature-dependent dissociation that is required for efficient substrate binding. Our analysis shows that Hsp25 and Hsp26 reacted in a similar manner with the nonnative proteins. For all substrates investigated, complexes of defined size and shape were formed. Interestingly, several different nonnative proteins could be incorporated into defined sHsp-substrate complexes. The first substrate protein bound seems to determine the complex morphology. Thus, despite the differences in quaternary structure and mode of activation, the formation of large uniform sHsp-substrate complexes seems to be a general feature of sHsps, and this unique chaperone mechanism is conserved from yeast to mammals.

* This work was supported by grants from the Deutsche Forschungsgemeinschaft (to J. B.), and the Fonds der Chemischen Industrie (to J. B. and M. G.).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.

Dagger Present address: Kendle GmbH & Co., GMI KG, Stefan-George-Ring 6, D-81929 Munich, Germany.

To whom correspondence should be addressed. Tel.: 49-89-289-13340; Fax: 49-89-289-13345; E-mail: johannes.buchner@ch.tum.de.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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