Deep conservation of prion-like composition in the eukaryotic prion-former Pub1/Tia1 family and its relatives

PeerJ

article

Wan-Chun Su¹  Paul M. Harrison¹ 

[1] Department of Biology, McGill University

关键词: Prion;    Pub1;    Tia1;    Nam8;    RNA-binding;    Compositional bias;    Intrinsic disorder;    Yeast;    Human;    Evolution;   

DOI  :  10.7717/peerj.9023

学科分类：社会科学、人文和艺术（综合）

来源: Inra

【 摘 要 】

Pub1 protein is an important RNA-binding protein functional in stress granule assembly in budding yeast Saccharomyces cerevisiae71% of the Nam8 family), but proteins with just one or two RRM domains occur frequently in some clades, indicating that these are not due to annotation errors. Overall, our results indicate that a basic scaffold comprising three RNA-binding domains and at least one prion-like region has been largely conserved since the last common ancestor of eukaryotes, providing further evidence that prion-like aggregation may be a very ancient and conserved phenomenon for certain specific proteins.

【 授权许可】

CC BY