Abstract
Proteins capable of self-perpetuating changes in conformation and function (known as prions) can serve as genetic elements. To test whether novel prions could be created by recombinant methods, a yeast prion determinant was fused to the rat glucocorticoid receptor. The fusion protein existed in different heritable functional states, switched between states at a low spontaneous rate, and could be induced to switch by experimental manipulations. The complete change in phenotype achieved by transferring a prion determinant from one protein to another confirms the protein-only nature of prion inheritance and establishes a mechanism for engineering heritable changes in phenotype that should be broadly applicable.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Fungal Proteins / chemistry*
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Fungal Proteins / genetics
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Fungal Proteins / metabolism*
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Genes, Reporter
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Guanidine / pharmacology
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Heat-Shock Proteins / pharmacology
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Peptide Termination Factors
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Phenotype
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Prions / chemistry*
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Prions / genetics
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Prions / metabolism*
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Rats
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Receptors, Glucocorticoid / chemistry
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Receptors, Glucocorticoid / genetics
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Receptors, Glucocorticoid / metabolism
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Saccharomyces cerevisiae / chemistry
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae Proteins*
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Transcription, Genetic
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Transformation, Genetic
Substances
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Fungal Proteins
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Heat-Shock Proteins
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Peptide Termination Factors
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Prions
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Receptors, Glucocorticoid
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Recombinant Fusion Proteins
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SUP35 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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HsP104 protein, S cerevisiae
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Guanidine