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dc.contributor.authorVillali, Janice
dc.contributor.authorDark, Jason
dc.contributor.authorBrechtel, Teal M
dc.contributor.authorPei, Fen
dc.contributor.authorSindi, Suzanne S
dc.contributor.authorSerio, Tricia R
dc.date.accessioned2020-06-03T18:40:49Z
dc.date.available2020-06-03T18:40:49Z
dc.date.issued2020-05-04
dc.identifier.citationVillali, 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/s41594-020-0416-6en_US
dc.identifier.issn1545-9993
dc.identifier.pmid32367069
dc.identifier.doi10.1038/s41594-020-0416-6
dc.identifier.urihttp://hdl.handle.net/10150/641508
dc.description.abstractAmyloid 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.en_US
dc.language.isoenen_US
dc.publisherNATURE PUBLISHING GROUPen_US
dc.rights© The Author(s), under exclusive licence to Springer Nature America, Inc. 2020.en_US
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/
dc.titleNucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeasten_US
dc.typeArticleen_US
dc.identifier.eissn1545-9985
dc.contributor.departmentUniv Arizona, Dept Mol & Cellular Biolen_US
dc.identifier.journalNATURE STRUCTURAL & MOLECULAR BIOLOGYen_US
dc.description.note6 month embargo; published online: 4 May 2020en_US
dc.description.collectioninformationThis 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.en_US
dc.eprint.versionFinal accepted manuscripten_US
dc.source.journaltitleNature structural & molecular biology
dc.source.countryUnited States
dc.source.countryUnited States


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