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Papers In Press, published online ahead of print March 12, 2003
J. Biol. Chem, 10.1074/jbc.M301640200
Submitted on February 17, 2003
Revised on March 11, 2003
Accepted on March 12, 2003

Analysis of the interaction of small heat shock proteins with unfolding proteins

Thusnelda Stromer, Monika Ehrnsperger, Matthias Gaestel, and Johannes Buchner

Institut fur Organische Chemie und Biochemie, Technische Universität München, Garching 85747

Corresponding Author: johannes.buchner{at}ch.tum.de

The ubiquitous small heat shock proteins (sHsp) are efficient molecular chaperones which 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 which is required for efficient substrate binding. Our analysis shows that Hsp25 and Hsp26 react in similar manner with the nonnative proteins. For all substrates investigated, complexes of defined size and shape are formed. Interestingly, several different nonnative proteins can be incorporated in defined substrate-sHsp 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 substrate-sHsp complexes seems to be a general feature of sHsp and this unique chaperone mechanism is conserved from yeast to mammals.


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