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A Systematic Survey Identifies Prions and Illuminates Sequence Features of Prionogenic Proteins
A bioinformatic proteome-wide survey for prionogenic proteins in S. cerevisiae found an unexpected amino acid bias in aggregation-prone candidates and discovered that 19 of these could also form prions. Expand
Prion-like Polymerization Underlies Signal Transduction in Antiviral Immune Defense and Inflammasome Activation
Results indicate that prion-like polymerization is a conserved signal transduction mechanism in innate immunity and inflammation. Expand
Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis
- Randal Halfmann, S. Lindquist
- Chemistry, Medicine
- Journal of visualized experiments : JoVE
- 16 July 2008
An adaptation of this technique that facilitates its use in large-scale applications, such as screens for novel prions and other amyloidogenic proteins, is demonstrated, which uses capillary transfer for greater reliability and ease of use, and allows any sized gel to be accomodated. Expand
Prions are a common mechanism for phenotypic inheritance in wild yeasts
- Randal Halfmann, Daniel F. Jarosz, Sandra K. Jones, Amelia Chang, A. Lancaster, S. Lindquist
- Biology, Medicine
- 1 February 2012
Biochemically test approximately 700 wild strains of Saccharomyces for [PSI+] or [MOT3+], and find these prions in many, and they conferred diverse phenotypes that were frequently beneficial under selective conditions. Expand
Heritable Remodeling of Yeast Multicellularity by an Environmentally Responsive Prion
It is reported that a prion formed by the Mot3 transcription factor, [MOT3(+)], governs the acquisition of facultative multicellularity in the budding yeast Saccharomyces cerevisiae, and these data demonstrate that prions can act as environmentally responsive molecular determinants of multICEllularity and contribute to the natural morphological diversity of budding yeast. Expand
Chaperone-dependent amyloid assembly protects cells from prion toxicity
- Peter M Douglas, Sebastian Treusch, +4 authors D. Cyr
- Biology, Medicine
- Proceedings of the National Academy of Sciences
- 20 May 2008
It is established that even subtle changes in the folding homeostasis of an amyloidogenic protein can create a severe proteotoxic gain-of-function phenotype and that chaperone-mediated amyloids assembly can be cytoprotective. Expand
Prions, protein homeostasis, and phenotypic diversity.
It is suggested that these qualities allow prions to act as 'bet-hedging' devices that facilitate the adaptation of yeasts to stressful environments, and might speed the evolution of new traits. Expand
Epigenetics in the Extreme: Prions and the Inheritance of Environmentally Acquired Traits
Prions are an unusual form of epigenetics: Their stable inheritance and complex phenotypes come about through protein folding rather than nucleic acid–associated changes. With intimate ties to… Expand
Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins.
This work uses cell biological, biochemical, and computational techniques to compare Q/N-rich protein variants, and finds that the two residues have strong and opposing effects: N richness promotes assembly of benign self-templating amyloids; Q richness promotes formation of toxic nonamyloid conformers. Expand
Biochemical, cell biological, and genetic assays to analyze amyloid and prion aggregation in yeast.
A range of biochemical, cell biological and yeast genetic methods that are currently used in the laboratory to study protein aggregation and the formation of amyloids and prions are provided. Expand