Abstract
Prions, infectious proteins, can transmit diseases or be the basis of heritable traits (or both), mostly based on amyloid forms of the prion protein. A single protein sequence can be the basis for many prion strains/variants, with different biological properties based on different amyloid conformations, each rather stably propagating. Prions are unique in that evolution and selection work at both the level of the chromosomal gene encoding the protein, and on the prion itself selecting prion variants. Here, we summarize what is known about the evolution of prion proteins, both the genes and the prions themselves. We contrast the one known functional prion, [Het-s] of Podospora anserina, with the known disease prions, the yeast prions [PSI+] and [URE3] and the transmissible spongiform encephalopathies of mammals.
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Abbreviations
- TSE:
-
Transmissible spongiform encephalopathy
- BSE:
-
Bovine spongiform encephalopathy
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Acknowledgments
This work was supported in part by the Intramural Program of the National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
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Genetic nomenclature
Yeast chromosomal genes are given as URE2, SUP35, RNQ1, BTN2, etc.
Non-chromosomal genes, such as yeast prions, are shown in brackets, such as [URE3], [PSI+], [PIN+], etc.
Proteins are shown as Ure2p, Sup35p, Rnq1p, etc.
Phenotypes are shown as Ade+ or Ura−.
For the Podospora anserina system, the [Het-s] prion is due to the HET-s protein.
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Wickner, R.B., Kelly, A.C. Prions are affected by evolution at two levels. Cell. Mol. Life Sci. 73, 1131–1144 (2016). https://doi.org/10.1007/s00018-015-2109-6
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DOI: https://doi.org/10.1007/s00018-015-2109-6