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Science. 1997 Jan 17;275(5298):387-9.

Functional specificity among Hsp70 molecular chaperones.

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  • 1Department of Biomolecular Chemistry, University of Wisconsin, Madison, WI 53706, USA. ecraig@facstaff.wisc.edu

Abstract

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.

PMID:
8994035
[PubMed - indexed for MEDLINE]
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