ArticleMolecular cell2013
Structural definition is important for the propagation of the yeast [PSI+] prion.
Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Cryo-EM structure of ex vivo Sup35 yeast prion and the factors defining prion phenotype.Nature communications · 2026Article
- A Prion-Like Domain in EBV EBNA1 Promotes Phase Separation and Enables SRRM1 Splicing.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- A viral expression factor behaves as a prion.Nature communications · 2019Article
- Molecular basis for diversification of yeast prion strain conformation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A dominant-negative mutant inhibits multiple prion variants through a common mechanism.PLoS genetics · 2017Article
- [PSI(+)] turns 50.Prion · 2015Article
- Review
- Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.PLoS pathogens · 2014Article
- Distinct prion strains are defined by amyloid core structure and chaperone binding site dynamics.Chemistry & biology · 2014Article
- Rebels with a cause: molecular features and physiological consequences of yeast prions.FEMS yeast research · 2014Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Prions are propagated in Saccharomyces cerevisiae with remarkable efficiency, yet we know little about the structural basis of sequence variations in the prion protein that support or prohibit propagation of the prion conformation. We show that certain single-amino-acid substitutions in the prion protein Sup35 impact negatively on the maintenance of the associated prion-based [PSI(+)] trait by combining in vivo phenotypic analysis with solution NMR structural studies. A clear correlation is observed between mutationally induced conformational differences in one of the oligopeptide repeats (R2) in the N terminus of Sup35 and the relative ability to propagate [PSI(+)]. Strikingly, substitution of one of a Gly-Gly pair with highly charged residues that significantly increase structural definition of R2 lead to a severe [PSI(+)] propagation defect. These findings offer a molecular explanation for the dominant-negative effects of such psi-no-more (PNM) mutations and demonstrate directly the importance of localized structural definition in prion propagation.
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Registered trials
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