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PMID:20435400
| Citation |
Bonomo, J, Welsh, JP, Manthiram, K and Swartz, JR (2010) Comparing the functional properties of the Hsp70 chaperones, DnaK and BiP. Biophys. Chem. 149:58-66 |
|---|---|
| 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. |
| Links |
PubMed PMC3175487 Online version:10.1016/j.bpc.2010.04.001 |
| Keywords |
Endoplasmic Reticulum/metabolism; Escherichia coli Proteins/chemistry; HSP70 Heat-Shock Proteins/chemistry; Heat-Shock Proteins/chemistry; Luciferases/chemistry; Protein Biosynthesis; Protein Folding; Protein Structure, Tertiary |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0006457: protein folding |
ECO:0000314: |
P |
Figure 4 demonstrates re-folding of luciferase. |
complete | ||||
See also
References
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