Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions.

ABSTRACT: Amyloidogenic proteins associated with a variety of unrelated diseases are typically capable of forming several distinct self-templating conformers. In prion diseases, these different structures, called prion strains (or variants), confer dramatic variation in disease pathology and transmission. Aggregate stability has been found to be a key determinant of the diverse pathological consequences of different prion strains. Yet, it remains largely unclear what other factors might account for the widespread phenotypic variation seen with aggregation-prone proteins. Here, we examined a set of yeast prion variants of the [RNQ+] prion that differ in their ability to induce the formation of another yeast prion called [PSI+]. Remarkably, we found that the [RNQ+] variants require different, non-cont

SUBMITTER: Stein KC 

PROVIDER: S-EPMC4014422 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature