Abstract
The [URE3] and [PSI(+)] prions are infectious amyloid forms of Ure2p and Sup35p. Several chaperones influence prion propagation: Hsp104p overproduction destabilizes [PSI(+)], whereas [URE3] is sensitive to excess of Ssa1p or Ydj1p. Here, we show that overproduction of the chaperone, Sse1p, can efficiently cure [URE3]. Sse1p and Fes1p are nucleotide exchange factors for Ssa1p. Interestingly, deletion of either SSE1 or FES1 completely blocked [URE3] propagation. In addition, deletion of SSE1 also interfered with [PSI(+)] propagation.
Publication types
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Research Support, N.I.H., Intramural
MeSH terms
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Adenosine Triphosphatases / genetics
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Adenosine Triphosphatases / metabolism
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Glutathione Peroxidase
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Guanine Nucleotide Exchange Factors / genetics
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Guanine Nucleotide Exchange Factors / metabolism*
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HSP110 Heat-Shock Proteins / genetics
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HSP110 Heat-Shock Proteins / metabolism*
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HSP40 Heat-Shock Proteins / genetics
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HSP40 Heat-Shock Proteins / metabolism
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HSP70 Heat-Shock Proteins / genetics
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HSP70 Heat-Shock Proteins / metabolism*
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Intracellular Signaling Peptides and Proteins / genetics
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Intracellular Signaling Peptides and Proteins / metabolism
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Point Mutation
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Prions / genetics
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Prions / metabolism*
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Saccharomyces cerevisiae / cytology
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
Substances
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FES1 protein, S cerevisiae
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Guanine Nucleotide Exchange Factors
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HSP110 Heat-Shock Proteins
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HSP40 Heat-Shock Proteins
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HSP70 Heat-Shock Proteins
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Intracellular Signaling Peptides and Proteins
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Prions
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SSE1 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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YDJ1 protein, S cerevisiae
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Glutathione Peroxidase
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URE2 protein, S cerevisiae
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Adenosine Triphosphatases
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SSA1 protein, S cerevisiae