Dataset Information


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

Similar Datasets

2014-01-01 | S-EPMC4739623 | BioStudies
2014-01-01 | S-EPMC4109904 | BioStudies
2014-01-01 | S-EPMC4014422 | BioStudies
2014-01-01 | S-EPMC4725586 | BioStudies
1000-01-01 | S-EPMC2575465 | BioStudies
1000-01-01 | S-EPMC516497 | BioStudies
2014-01-01 | S-EPMC4601363 | BioStudies
2013-01-01 | S-EPMC3684756 | BioStudies
2019-01-01 | S-EPMC6422386 | BioStudies
2012-01-01 | S-EPMC3520751 | BioStudies