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Wickner, Reed B.; Edskes, Herman K.; Ross, Eric D.; Pierce, Michael M.; Shewmaker, Frank; Baxa, Ulrich und Brachmann, Andreas ORCID logoORCID: https://orcid.org/0000-0001-7980-8173 (2004): Prions of Yeast Are Genes Made of Protein: Amyloids and Enzymes. In: Cold Spring Harbor Symposia on Quantitative Biology, Bd. 69: S. 489-496

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Abstract

In 1994 we described two infectious proteins (prions) of Saccharomyces cerevisiae, showing that the nonchromosomal genes [URE3] and [PSI] are inactive, self-propagating forms of Ure2p and Sup35p, respectively (Wickner 1994). Since then, [Het-s], a prion of Podospora anserina (Coustou et al. 1997), and [PIN+], another S. cerevisiae prion (Derkatch et al. 1997, 2001; Sondheimer and Lindquist 2000), have been found. All of the above prions are based on self-propagating amyloids. Recently, we described another prion, called [β], which is based on the trans self-activation by the yeast vacuolar protease B (Roberts and Wickner 2003). Evidence has appeared suggesting that C, the non-Mendelian gene of Podospora anserina determining Crippled Growth, is also a self-activating prion of a MAP kinase kinase kinase (Kicka and Silar 2004). Study of these yeast and fungal phenomena has established that proteins can be genes and infectious entities and has revealed many details of what makes a protein infectious.

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