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Functional Specificity Among Hsp70 Molecular Chaperones

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Science  17 Jan 1997:
Vol. 275, Issue 5298, pp. 387-389
DOI: 10.1126/science.275.5298.387

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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.

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