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Science 17 January 1997:
Vol. 275. no. 5298, pp. 387 - 389
DOI: 10.1126/science.275.5298.387
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Reports

Functional Specificity Among Hsp70 Molecular Chaperones

Philip James, Christine Pfund, Elizabeth A. Craig *

Molecular chaperones of the 70-kilodalton heat shock protein (Hsp70) class bind to partially unfolded polypeptide substrates and participate in a wide variety of cellular processes. Differences in peptide-binding specificity among Hsp70s have led to the hypothesis that peptide binding determines specific Hsp70 functions. Protein domains were identified that were required for two separate functions of a yeast Hsp70 family. The peptide-binding domain was not required for either of these specific Hsp70 functions, which suggests that peptide-binding specificity plays little or no role in determining Hsp70 functions in vivo.

Department of Biomolecular Chemistry, University of Wisconsin, Madison, WI 53706, USA.
*   To whom correspondence should be addressed. E-mail: ecraig{at}facstaff.wisc.edu

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