Comparing the functional properties of the Hsp70 chaperones, DnaK and BiP
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 predominately provides folding assistance that is contemporaneous with translation.
Additional Information
© 2010 Elsevier. Received 15 March 2010, Revised 5 April 2010, Accepted 5 April 2010, Available online 10 April 2010. The authors would like to thank Dr. Linda Hendershot, St. Jude Children's Hospital, Memphis, TN and George Georgiou, University of Texas at Austin for providing several of the plasmids that were used in this work. The authors also thank Alyssa Bingham and Edwina Lai for assistance with the protein refolding and chaperone ATPase activity assays, respectively. This work was supported by NIH R21 grant GM077508-02.Additional details
- Eprint ID
- 114638
- DOI
- 10.1016/j.bpc.2010.04.001
- Resolver ID
- CaltechAUTHORS:20220505-565540000
- GM077508-02
- NIH
- Created
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2022-05-06Created from EPrint's datestamp field
- Updated
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2022-05-06Created from EPrint's last_modified field