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Reference: Edskes HK, et al. (2009) Prion variants and species barriers among Saccharomyces ure2 proteins. Genetics 181(3):1159-67

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Abstract

As hamster scrapie cannot infect mice, due to sequence differences in their PrP proteins, we find 'species barriers' to transmission of the [URE3] prion in Saccharomyces cerevisiae among Ure2 proteins of Saccharomyces cerevisiae, paradoxus, bayanus, cariocanus, and mikatae based on differences among their Ure2p prion domain sequences. The rapid variation of the N-terminal Ure2p prion domains results in protection against the detrimental effects of infection by a prion, just as the PrP residue 129 Met/Val polymorphism may have arisen to protect humans from the effects of cannibalism. Just as spread of bovine spongiform encephalopathy prion variant is less impaired by species barriers than is sheep scrapie, we find that some [URE3] prion variants are infectious to another yeast species while other variants (with the identical amino acid sequence) are not. The species barrier is thus prion variant-dependent as in mammals. [URE3] prion variant characteristics are maintained even on passage through the Ure2p of another species. Ure2p of S. castellii has a N-terminal Q/N rich 'prion domain' but does not form prions (in S. cerevisiae) and is not infected with [URE3] from Ure2p of other Saccharomyces. This implies that conservation of its 'prion domain' is not for the purpose of forming prions. Indeed the Ure2p prion domain has been shown to be important, though not essential, for the nitrogen catabolism regulatory role of the protein.

Reference Type
Journal Article
Authors
Edskes HK, McCann L, Hebert A, Wickner RB
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