Global analysis of protein aggregation in yeast during physiological conditions and arsenite stress.

ABSTRACT: Protein aggregation is a widespread phenomenon in cells and associated with pathological conditions. Yet, little is known about the rules that govern protein aggregation in living cells. In this study, we biochemically isolated aggregation-prone proteins and used computational analyses to identify characteristics that are linked to physiological and arsenite-induced aggregation in living yeast cells. High protein abundance, extensive physical interactions, and certain structural properties are positively correlated with an increased aggregation propensity. The aggregated proteins have high translation rates and are substrates of ribosome-associated Hsp70 chaperones, indicating that they are susceptible for aggregation primarily during translation/folding. The aggregation-prone proteins are

SUBMITTER: Ibstedt S 

PROVIDER: S-EPMC4197440 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature