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.

中文翻译：

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有核种子的大小决定了淀粉样蛋白的清除率，并为酵母中病毒的出现建立了障碍。

淀粉样蛋白的出现是罕见的事件，在其他聚集蛋白的存在下会被促进。人们认为这些聚集体是通过模板化具有胜任能力的成核种子而起作用的，但是我们发现它们在淀粉样蛋白出现后增强持久性方面具有意想不到的作用。具体来说，酿酒酵母Rnq1淀粉样蛋白减少了伴侣介导的Sup35淀粉样蛋白的分解，从而促进了其在酵母中的持久性。数学建模和相应的体内实验将淀粉样蛋白的持久性与Sup35成核种子的构象确定的大小联系起来，并表明淀粉样蛋白可通过在低于此阈值的条件下分解而被主动清除，从而抑制体内[PSI +] pr病毒的出现。值得注意的是，该框架解决了酵母pr病毒的外观和固化过程中的多个已知不一致问题。从而，