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Biophys Chem. 2010 Jun;149(1-2):58-66. doi: 10.1016/j.bpc.2010.04.001. Epub 2010 Apr 10.

Comparing the functional properties of the Hsp70 chaperones, DnaK and BiP.

Author information

1
Department of Chemical Engineering, Stanford University, 381 North-South Mall, Stanford, CA 94305-5025, USA. jeanne.bonomo@gmail.com

Abstract

The Hsp70 family of molecular chaperones is an essential class of chaperones that is present in many different cell types and cellular compartments. We have compared the bioactivities of the prokaryotic cytosolic Hsp70, DnaK, to that of the eukaryotic Hsp70, BiP, located in the endoplasmic reticulum (ER). Both chaperones helped to prevent protein aggregation. However, only DnaK provided enhanced refolding of denatured proteins. We also tested chaperone folding assistance during translation in the context of cell-free protein synthesis reactions for several protein targets and show that both DnaK and BiP can provide folding assistance under these conditions. Our results support previous reports suggesting that DnaK provides both post-translational and co-translational folding assistance while BiP predominantly provides folding assistance that is contemporaneous with translation.

PMID:
20435400
PMCID:
PMC3175487
DOI:
10.1016/j.bpc.2010.04.001
[Indexed for MEDLINE]
Free PMC Article

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