Measuring protein stability in the GroEL chaperonin cage reveals massive destabilization
- Weizmann Institute of Science, Israel
Abstract
The thermodynamics of protein folding in bulk solution have been thoroughly investigated for decades. By contrast, measurements of protein substrate stability inside the GroEL/ES chaperonin cage have not been reported. Such measurements require stable encapsulation, i.e. no escape of the substrate into bulk solution during experiments, and a way to perturb protein stability without affecting the chaperonin system itself. Here, by establishing such conditions, we show that protein stability in the chaperonin cage is reduced dramatically by more than 5 kcal mol-1 compared to that in bulk solution. Given that steric confinement alone is stabilizing, our results indicate that hydrophobic and/or electrostatic effects in the cavity are strongly destabilizing. Our findings are consistent with the iterative annealing mechanism of action proposed for the chaperonin GroEL.
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All data generated or analyses during this study are included in the manuscript file.
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Funding
United States-Israel Binational Science Foundation (2015170)
- Amnon Horovitz
Minerva Foundation
- Amnon Horovitz
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
Copyright
© 2020, Korobko et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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Measuring protein stability in the GroEL chaperonin cage reveals massive destabilization
eLife 9:e56511.
https://doi.org/10.7554/eLife.56511
