The concept of a prion as an infectious self-propagating protein isoform was initially
proposed to explain certain mammalian diseases. It is now clear that yeast also has …

Abstract Changes in protein conformation drive most biological processes, but none have
seized the imagination of scientists and the public alike as have the self-replicating …

Prions are a paradigm-shifting mechanism of inheritance in which phenotypes are encoded
by self-templating protein conformations rather than nucleic acids. Here, we examine the …

Prion proteins have the unusual capacity to fold into two functionally distinct conformations,
one of which is self-perpetuating. When yeast prion proteins switch state, they produce …

The yeast [PSI+] determinant is related to formation of large prion-like aggregates of the
conformationally altered Sup35 protein. Here, we show that these aggregates are composed …

A principle that has emerged from studies of protein aggregation is that proteins typically can
misfold into a range of different aggregated forms. Moreover, the phenotypic and …

Hsp100 and Hsp70 chaperones in bacteria, yeast, and plants cooperate to reactivate
aggregated proteins. Disaggregation relies on Hsp70 function and on ATP-dependent …

A long-standing goal of amyloid research has been to characterize the structural basis of the
rate-determining nucleating event. However, the ephemeral nature of nucleation has made …

Prion proteins undergo self-sustaining conformational conversions that heritably alter their
activities. Many of these proteins operate at pivotal positions in determining how genotype is …

▪ Abstract Fungal prions are fascinating protein-based genetic elements. They alter cellular
phenotypes through self-perpetuating changes in protein conformation and are …