The effects of glutamine/asparagine content on aggregation and heterologous prion induction by yeast prion-like domains.

ABSTRACT: Prion-like domains are low complexity, intrinsically disordered domains that compositionally resemble yeast prion domains. Many prion-like domains are involved in the formation of either functional or pathogenic protein aggregates. These aggregates range from highly dynamic liquid droplets to highly ordered detergent-insoluble amyloid-like aggregates. To better understand the amino acid sequence features that promote conversion to stable, detergent-insoluble aggregates, we used the prediction algorithm PAPA to identify predicted aggregation-prone prion-like domains with a range of compositions. While almost all of the predicted aggregation-prone domains formed foci when expressed in cells, the ability to form the detergent-insoluble aggregates was highly correlated with glutamine/asparagin

SUBMITTER: Shattuck JE 

PROVIDER: S-EPMC5553303 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature