Abstract
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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Amyloid / metabolism
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Asparagine / metabolism
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Cytosol / metabolism
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Genome, Fungal
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Glutamine / metabolism
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Heat-Shock Proteins / metabolism
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Molecular Sequence Data
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Peptide Termination Factors
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Phenotype
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Prions / analysis*
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Prions / chemistry
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Prions / genetics
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Prions / metabolism
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Proteome / analysis*
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / analysis*
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Saccharomyces cerevisiae Proteins / chemistry
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism
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Transcription Factors / chemistry
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Transcription Factors / metabolism
Substances
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Amyloid
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Heat-Shock Proteins
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MOT3 protein, S cerevisiae
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Peptide Termination Factors
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Prions
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Proteome
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SUP35 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Transcription Factors
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Glutamine
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HsP104 protein, S cerevisiae
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Asparagine