A unifying model for the propagation of prion proteins in yeast brings insight into the [PSI+] prion.

ABSTRACT: The use of yeast systems to study the propagation of prions and amyloids has emerged as a crucial aspect of the global endeavor to understand those mechanisms. Yeast prion systems are intrinsically multi-scale: the molecular chemical processes are indeed coupled to the cellular processes of cell growth and division to influence phenotypical traits, observable at the scale of colonies. We introduce a novel modeling framework to tackle this difficulty using impulsive differential equations. We apply this approach to the [PSI+] yeast prion, which is associated with the misconformation and aggregation of Sup35. We build a model that reproduces and unifies previously conflicting experimental observations on [PSI+] and thus sheds light onto characteristics of the intracellular molecular processe

SUBMITTER: Lemarre P 

PROVIDER: S-EPMC7274466 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature