PMID:9829996
| Citation |
Llorca, O, Galán, A, Carrascosa, JL, Muga, A and Valpuesta, JM (1998) GroEL under heat-shock. Switching from a folding to a storing function. J. Biol. Chem. 273:32587-94 |
|---|---|
| Abstract |
Chaperonin GroEL from Escherichia coli, together with its cochaperonin GroES, are proteins involved in assisting the folding of polypeptides. GroEL is a tetradecamer composed of two heptameric rings, which enclose a cavity where folding takes place through multiple cycles of substrate and GroES binding and release. GroEL and GroES are also heat-shock proteins, their synthesis being increased during heat-shock conditions to help the cell coping with the thermal stress. Our results suggest that, as the temperature increases, GroEL decreases its protein folding activity and starts acting as a "protein store." The molecular basis of this behavior is the loss of inter-ring signaling, which slows down GroES liberation from GroEL and therefore the release of the unfolded protein from the GroEL cavity. This behavior is reversible, and after heat-shock, GroEL reverts to its normal function. This might have a physiological meaning, since under thermal stress conditions, it may be inefficient for the cell to fold thermounstable proteins that are prone to denaturation. |
| Links | |
| Keywords |
Adenosine Triphosphatases/metabolism; Chaperonin 60/metabolism; Escherichia coli/metabolism; Heat-Shock Response; Hot Temperature; Protein Folding |
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