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    Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast

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    Villali_Dark_etal_2020_merged.pdf
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    Author
    Villali, Janice
    Dark, Jason
    Brechtel, Teal M
    Pei, Fen
    Sindi, Suzanne S
    Serio, Tricia R
    Affiliation
    Univ Arizona, Dept Mol & Cellular Biol
    Issue Date
    2020-05-04
    
    Metadata
    Show full item record
    Publisher
    NATURE PUBLISHING GROUP
    Citation
    Villali, J., Dark, J., Brechtel, T.M. et al. Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast. Nat Struct Mol Biol (2020). https://doi.org/10.1038/s41594-020-0416-6
    Journal
    NATURE STRUCTURAL & MOLECULAR BIOLOGY
    Rights
    © The Author(s), under exclusive licence to Springer Nature America, Inc. 2020.
    Collection Information
    This item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.
    Abstract
    Amyloid appearance is a rare event that is promoted in the presence of other aggregated proteins. These aggregates were thought to act by templating the formation of an assembly-competent nucleation seed, but we find an unanticipated role for them in enhancing the persistence of amyloid after it arises. Specifically, Saccharomyces cerevisiae Rnq1 amyloid reduces chaperone-mediated disassembly of Sup35 amyloid, promoting its persistence in yeast. Mathematical modeling and corresponding in vivo experiments link amyloid persistence to the conformationally defined size of the Sup35 nucleation seed and suggest that amyloid is actively cleared by disassembly below this threshold to suppress appearance of the [PSI+] prion in vivo. Remarkably, this framework resolves multiple known inconsistencies in the appearance and curing of yeast prions. Thus, our observations establish the size of the nucleation seed as a previously unappreciated characteristic of prion variants that is key to understanding transitions between prion states.
    Note
    6 month embargo; published online: 4 May 2020
    ISSN
    1545-9993
    EISSN
    1545-9985
    PubMed ID
    32367069
    DOI
    10.1038/s41594-020-0416-6
    Version
    Final accepted manuscript
    ae974a485f413a2113503eed53cd6c53
    10.1038/s41594-020-0416-6
    Scopus Count
    Collections
    UA Faculty Publications

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