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Concept
Fungal prion
Summary
A fungal prion is a prion that infects hosts which are fungi. Fungal prions are naturally occurring proteins that can switch between multiple, structurally distinct conformations, at least one of which is self-propagating and transmissible to other prions. This transmission of protein state represents an epigenetic phenomenon where information is encoded in the protein structure itself, instead of in nucleic acids. Several prion-forming proteins have been identified in fungi, primarily in the yeast Saccharomyces cerevisiae. These fungal prions are generally considered benign, and in some cases even confer a selectable advantage to the organism.
Fungal prions have provided a model for the understanding of disease-forming mammalian prions. Study of fungal prions has led to a characterisation of the sequence features and mechanisms that enable prion domains to switch between functional and amyloid-forming states.
Prions are formed by portable, transmissible prion domains that are often enriched in asparagine, glutamine, tyrosine and glycine residues. When a reporter protein is fused with a prion domain, it forms a chimeric protein that demonstrates the conformational switching that is characteristic of prions. Meanwhile, removing this prion domain prevents prionogenesis. This suggests that these prion domains are, in fact, portable and are the sole initiator of prionogenesis. This supports the protein-only hypothesis.
A recent study of candidate prion domains in S. cerevisiae found several specific sequence features that were common to proteins showing aggregation and self-templating properties. For example, proteins that aggregated had candidate prion domains that were more highly enriched in asparagine, while non-aggregating domains where more highly enriched in glutamine and charged peptides. There was also evidence that the spacing of charged peptides that prevent amyloid formation, such as proline, is important in prionogenesis.
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