Yeast Short-Lived Actin-Associated Protein Forms a Metastable Prion in Response to Thermal Stress.

ABSTRACT: Self-perpetuating ordered protein aggregates (amyloids and prions) are associated with a variety of neurodegenerative disorders. Although environmental agents have been linked to certain amyloid diseases, the molecular basis of their action remains unclear. We have employed endogenous yeast prions as a model system to study environmental control of amyloid formation. A short-lived actin-associated yeast protein Lsb2 can trigger prion formation by other proteins in a mode regulated by the cytoskeleton and ubiquitin-dependent processes. Here, we show that such a heterologous prion induction is due to the ability of Lsb2 to form a transient prion state, generated in response to thermal stress. Evolutionary acquisition of prion-inducing activity by Lsb2 is traced to a single amino acid change,

SUBMITTER: Chernova TA 

PROVIDER: S-EPMC5267347 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature