Dictyostelium discoideum has a highly Q/N-rich proteome and shows an unusual resilience to protein aggregation.

ABSTRACT: Many protein-misfolding diseases are caused by proteins carrying prion-like domains. These proteins show sequence similarity to yeast prion proteins, which can interconvert between an intrinsically disordered and an aggregated prion state. The natural presence of prions in yeast has provided important insight into disease mechanisms and cellular proteostasis. However, little is known about prions in other organisms, and it is not yet clear whether the findings in yeast can be generalized. Using bioinformatics tools, we show that Dictyostelium discoideum has the highest content of prion-like proteins of all organisms investigated to date, suggesting that its proteome has a high overall aggregation propensity. To study mechanisms regulating these proteins, we analyze the behavior of several

SUBMITTER: Malinovska L 

PROVIDER: S-EPMC4443358 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature