Journal
CELL
Volume 137, Issue 1, Pages 146-158Publisher
CELL PRESS
DOI: 10.1016/j.cell.2009.02.044
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Funding
- G. Harold and Leila Y. Mathers Foundation
- NIH [GM025874]
- HHMI
- Deutsche Forschungsgemeinschaft (DFG)
- NSF
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Prions are proteins that convert between structurally and functionally distinct states, one or more of which is transmissible. In yeast, this ability allows them to act as non-Mendelian elements of phenotypic inheritance. To further our understanding of prion biology, we conducted a bioinformatic proteome-wide survey for prionogenic proteins in S. cerevisiae, followed by experimental investigations of 100 prion candidates. We found an unexpected amino acid bias in aggregation-prone candidates and discovered that 19 of these could also form prions. At least one of these prion proteins, Mot3, produces a bona fide prion in its natural context that increases population-level phenotypic heterogeneity. The self-perpetuating states of these proteins present a vast source of heritable phenotypic variation that increases the adaptability of yeast populations to diverse environments.
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