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PMID:2528694
| Citation |
Ostermann, J, Horwich, AL, Neupert, W and Hartl, FU (1989) Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature 341:125-30 |
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| Abstract |
Mitochondrial heat-shock protein hsp60 functions in the folding of proteins imported into mitochondria. Folding occurs at the surface of hsp60 in an ATP-mediated reaction, followed by release of the bound polypeptides. We propose that hsp60 catalyses protein folding. |
| Links |
PubMed Online version:10.1038/341125a0 |
| Keywords |
Adenosine Triphosphate/metabolism; Animals; Ethylmaleimide/pharmacology; Heat-Shock Proteins/metabolism; Humans; Kinetics; Mitochondria/drug effects; Mitochondria/metabolism; Neurospora/enzymology; Protein Conformation; Proton-Translocating ATPases/metabolism; Tetrahydrofolate Dehydrogenase/metabolism |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0006457: protein folding |
ECO:0000314: |
P |
As seen in figure 4a, addition of ATP is required for proper release and folding into protease resistant conformation of protein from hsp60 |
complete | ||||
See also
References
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