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Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilities.


ABSTRACT: Variation in amyloid structures profoundly influences a wide array of pathological phenotypes in mammalian protein conformation disorders and dominantly inherited phenotypes in yeast. Here, we describe, for the first time, naturally occurring, self-propagating, structural variants of a prion protein isolated from wild strains of the yeast Saccharomyces cerevisiae. Variants of the [RNQ?] prion propagating in a variety of wild yeast differ biochemically, in their intracellular distributions, and in their ability to promote formation of the [PSI?] prion. [PSI?] is an epigenetic regulator of cellular phenotype and adaptability. Strikingly, we find that most natural [RNQ?] variants induced [PSI?] at high frequencies and the majority of [PSI?] variants elicited strong cellular phenotypes. We hypothesize that the presence of an efficient [RNQ?] template primes the cell for [PSI?] formation in order to induce [PSI?] in conditions where it would be advantageous. These studies utilize naturally occurring structural variants to expand our understanding of the consequences of diverse prion conformations on cellular phenotypes.

SUBMITTER: Westergard L 

PROVIDER: S-EPMC4708258 | BioStudies | 2014-01-01

REPOSITORIES: biostudies

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