ArticlePloS one2012
The effects of amino acid composition of glutamine-rich domains on amyloid formation and fragmentation.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 41 citations in OpenAlex.
- Cryo-EM structure of ex vivo Sup35 yeast prion and the factors defining prion phenotype.Nature communications · 2026Article
- Deletion Analysis of Phase Separation, Amyloid Formation and Prion Propagation by the Intrinsically Disordered Region of Yeast Sup35 Protein.International journal of molecular sciences · 2026Article
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- How Big Is the Yeast Prion Universe?International journal of molecular sciences · 2023Review
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- Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022Review
- Amyloid Fragmentation and Disaggregation in Yeast and Animals.Biomolecules · 2021Review
- From Prions to Stress Granules: Defining the Compositional Features of Prion-Like Domains That Promote Different Types of Assemblies.International journal of molecular sciences · 2021Review
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- Article
- Yeast Sup35 Prion Structure: Two Types, Four Parts, Many Variants.International journal of molecular sciences · 2019Article
- Article
- Chaperone functional specificity promotes yeast prion diversity.PLoS pathogens · 2018Article
- Article
- Melanosomal formation of PMEL core amyloid is driven by aromatic residues.Scientific reports · 2017Article
- Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo.PLoS genetics · 2016Article
- A glass menagerie of low complexity sequences.Current opinion in structural biology · 2016Review
- A protein polymerization cascade mediates toxicity of non-pathological human huntingtin in yeast.Scientific reports · 2015Article
- Distinct amino acid compositional requirements for formation and maintenance of the [PSI⁺] prion in yeast.Molecular and cellular biology · 2015Article
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Fragmentation of amyloid polymers by the chaperone Hsp104 allows them to propagate as prions in yeast. The factors which determine the frequency of fragmentation are unclear, though it is often presumed to depend on the physical strength of prion polymers. Proteins with long polyglutamine stretches represent a tractable model for revealing sequence elements required for polymer fragmentation in yeast, since they form poorly fragmented amyloids. Here we show that interspersion of polyglutamine stretches with various amino acid residues differentially affects the in vivo formation and fragmentation of the respective amyloids. Aromatic residues tyrosine, tryptophan and phenylalanine strongly stimulated polymer fragmentation, leading to the appearance of oligomers as small as dimers. Alanine, methionine, cysteine, serine, threonine and histidine also enhanced fragmentation, while charged residues, proline, glycine and leucine inhibited polymerization. Our data indicate that fragmentation frequency primarily depends on the recognition of fragmentation-promoting residues by Hsp104 and/or its co-chaperones, rather than on the physical stability of polymers. This suggests that differential exposure of such residues to chaperones defines prion variant-specific differences in polymer fragmentation efficiency.
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Registered trials
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