Abstract
Prions are self‐perpetuating proteins able to switch between a soluble state and an aggregated‐and‐transmissible conformation. These proteinaceous entities have been widely studied in yeast, where they are involved in hereditable phenotypic adaptations. The notion that such proteins could play functional roles and be positively selected by evolution has triggered the development of computational tools to identify prion‐like proteins in different kingdoms of life. These algorithms have succeeded in screening multiple proteomes, allowing the identification of prion‐like proteins in a diversity of unrelated organisms, evidencing that the prion phenomenon is well conserved among species. Interestingly enough, prion‐like proteins are not only connected with the formation of functional membraneless protein–nucleic acid coacervates, but are also linked to human diseases. This review addresses state‐of‐the‐art computational approaches to identify prion‐like proteins, describes proteome‐wide analysis efforts, discusses these unique proteins' functional role, and illustrates recently validated examples in different domains of life.
Highlights
Prions are self-perpetuating proteins able to switch between a soluble state and an aggregated-and-transmissible conformation
FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies
The proteome studies discussed in this review make clear that the list of identified proteins bearing prion-like domain (PrLD) will be steadily increasing and that they are widespread in all life forms, even in viruses
Summary
Departament de Bioquımica i Biologia Molecular, Institut de Biotecnologia i de Biomedicina, Universitat Autonoma de Barcelona, Spain. The extensive research devoted to the characterization of the PrDs of the yeast prions Sup and Ure2p (their prionogenic states are known as [PSI+] and [URE3], respectively) has enabled to dissect the different molecular determinants behind prion conversion [1518] This knowledge has fueled the development of a collection of bioinformatics tools to identify proteins bearing similar prion-like domains (PrLDs) in biological relevant sequence databases as well as in complete proteomes [13,14,19,20,21,22,23,24,25,26,27]. The method, named prion RANKing and classification (pRANK), was trained on top of 22 known Q/N rich yeast PrDs in the
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