Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 73, Issue 6, Pages 1131-1144Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-015-2109-6
Keywords
Amyloid; Ure2p; Sup35p; HET-s; Rnq1; Parallel in-register beta sheet
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Funding
- National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
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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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