Department of Medical Genome Sciences, Graduate School of Frontier Sciences, University of Tokyo, Kashiwanoha, Kashiwa, Chiba, Japan.
FEBS J. 2010 Mar;277(6):1359-68. doi: 10.1111/j.1742-4658.2010.07569.x. Epub 2010 Feb 9.
Prions are infectious proteins, in which self-propagating amyloid conformations of proteins are transmitted. The budding yeast Saccharomyces cerevisiae, one of the best-studied model eukaryotes, also has prions, and thus provides a tractable model system with which to understand the mechanisms of prion phenomena. The yeast prions are protein-based heritable elements, such as [PSI(+)], in which aggregates of prion proteins are transmitted to daughter cells in a non-Mendelian manner. Although the genetic approaches preceded the yeast prion studies, recent investigations of the dynamic aspects of the prion proteins have unraveled the molecular mechanisms by which prions are propagated and transmitted. In particular, several lines of evidence have revealed that the oligomeric species of prion proteins dispersed in the cytoplasm are critical for the transmission. This review summarizes the topics on the transmissible entities of yeast prions, focusing mainly on the Sup35 protein in [PSI(+)].
朊病毒是传染性蛋白，其中蛋白质的自我传播淀粉样构象被传递。 budding 酵母 Saccharomyces cerevisiae 是研究最深入的模式真核生物之一，也有朊病毒，因此提供了一个易于处理的模型系统，可用于理解朊病毒现象的机制。酵母朊病毒是基于蛋白质的可遗传元件，例如 [PSI(+)]，其中朊病毒蛋白的聚集体以非孟德尔方式传递给子细胞。尽管遗传方法先于酵母朊病毒研究，但最近对朊病毒蛋白动态方面的研究揭示了朊病毒传播和传递的分子机制。特别是，有几条证据表明，分散在细胞质中的朊病毒蛋白的寡聚体物种对于传递至关重要。这篇综述总结了酵母朊病毒可传播实体的主题，主要集中在 [PSI(+)]中的 Sup35 蛋白上。
