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Originally published In Press as doi:10.1074/jbc.M205800200 on September 15, 2002

J. Biol. Chem., Vol. 277, Issue 48, 46026-46034, November 29, 2002
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Hsp31, the Escherichia coli yedU Gene Product, Is a Molecular Chaperone Whose Activity Is Inhibited by ATP at High Temperatures*

M. S. R. Sastry, Konstantin Korotkov§, Yan Brodsky, and François BaneyxDagger

From the Department of Chemical Engineering, University of Washington, Seattle, Washington 98195-1750

The Escherichia coli chromosome contains several uncharacterized heat-inducible loci that may encode novel molecular chaperones or proteases. Here we show that the 31-kDa product of the yedU gene is an efficient homodimeric molecular chaperone that is conserved in a number of pathogenic eubacteria and fungi. Heat shock protein (Hsp) 31 relies on temperature-driven conformational changes to expose structured hydrophobic domains that are likely responsible for substrate binding. Complementing the function of refolding, remodeling, and holding chaperones, Hsp 31 preferentially interacts with early unfolding intermediates and rapidly releases them in an active form after transfer to low temperatures. Although Hsp 31 does not appear to exhibit intrinsic ATPase activity, binding of ATP at high temperatures restricts the size or availability of the substrate binding site, thereby modulating chaperone activity. The possible role of ATP in coordinating the function of the cellular complement of molecular chaperones is discussed.

* This work was supported by Research Project Grant MBC-99-335-01 from the American Cancer Society.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 To whom correspondence should be addressed: Dept. of Chemical Engineering, Box 351750, University of Washington, Seattle, WA 98195-1750. Tel.: 206-685-7659; Fax: 206-685-3451; E-mail: baneyx@u.washington.edu.

§ Present address: Dept. of Biochemistry, Box 357742, University of Washington, Seattle, WA 98195-1750.

Present address: Immunex, 51 University St., Seattle, WA 98101.

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