The copper transport-associated protein Ctr4 can form prion-like epigenetic determinants in Schizosaccharomyces pombe

What is it about?

Although several prions have been widely studied in budding yeast, the only other fungal prion described so far is from the filamentous fungus, Podospora anserina. In this manuscript, we present evidence for a prion-forming protein in fission yeast. We show that fission yeast not only has the cellular machinery to allow a heterologous prion – the [PSI+] prion from budding yeast – to form and propagate, but also has at least one endogenous protein, Ctr4, that satisfies the key criteria that define prions, with the potential to form a protein-based epigenetic determinant that can impact the phenotype of the host. The Ctr4-based [CTR+] prion identified in this study present an important step towards establishing fission yeast as a model system for this unique form of protein-based inheritance.

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Why is it important?

Prions are protein-based infectious entities associated with fatal brain diseases in animals, but also modify a range of host-cell phenotypes in the budding yeast. The amyloid forms of prions are also characteristic of the protein aggregates deposited in the brains of Alzheimer’s, Parkinson’s, and Huntington’s Disease patients. Although the potential for transmission was initially uncovered for prions, recent studies suggest the prion-like spread of a number of other amyloid-based protein aggregates in many neurodegenerative pathologies. Many questions remain about the evolution and biology of prions. The Ctr4-based [CTR+] prion identified here is a first step towards establishing fission yeast as a model system for this unique form of protein-based inheritance which may be much more widespread than suggested by the low number of species in which prions have been described and studied so far.