Mechanisms for curing yeast prions
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ijms-21-06536.pdf
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1.64 MB
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Author(s)
Greene, Lois E.
Saba, Farrin
Silberman, Rebecca Estelle
Zhao, Xiaohong
Date Issued
September 2020
Journal
International Journal of Molecular Sciences
Publisher
Multidisciplinary Digital Publishing Institute
Citation
Greene, Lois E. et al. "Mechanisms for curing yeast prions." International Journal of Molecular Sciences 21, 18 (September 2020): 6536 ©2020 Author(s)
Version
Final published version
Abstract
Prions are infectious proteins that self-propagate by changing from their normal folded conformation to a misfolded conformation. The misfolded conformation, which is typically rich in β-sheet, serves as a template to convert the prion protein into its misfolded conformation. In yeast, the misfolded prion proteins are assembled into amyloid fibers or seeds, which are constantly severed and transmitted to daughter cells. To cure prions in yeast, it is necessary to eliminate all the prion seeds. Multiple mechanisms of curing have been found including inhibiting severing of the prion seeds, gradual dissolution of the prion seeds, asymmetric segregation of the prion seeds between mother and daughter cells during cell division, and degradation of the prion seeds. These mechanisms, achieved by using different protein quality control machinery, are not mutually exclusive; depending on conditions, multiple mechanisms may work simultaneously to achieve curing. This review discusses the various methods that have been used to differentiate between these mechanisms of curing.
MIT Department
Koch Institute for Integrative Cancer Research at MIT
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Creative Commons Attribution
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DOI of Published Version
https://doi.org/10.3390/ijms21186536
