Derkatch I L, Bradley M E, Hong J Y, Liebman S W
Laboratory for Molecular Biology, Department of Biological Sciences, University of Illinois at Chicago, 900 South Ashland Avenue, Chicago, IL 60607, USA.
Cell. 2001 Jul 27;106(2):171-82. doi: 10.1016/s0092-8674(01)00427-5.
Prions are self-propagating protein conformations. Recent research brought insight into prion propagation, but how they first appear is unknown. We previously established that the yeast non-Mendelian trait [PIN(+)] is required for the de novo appearance of the [PSI(+)] prion. Here, we show that the presence of prions formed by Rnq1 or Ure2 is sufficient to make cells [PIN(+)]. Thus, [PIN(+)] can be caused by more than one prion. Furthermore, an unbiased functional screen for [PIN(+)] prions uncovered the known prion gene, URE2, the proposed prion gene, NEW1, and nine novel candidate prion genes all carrying prion domains. Importantly, the de novo appearance of Rnq1::GFP prion aggregates also requires the presence of other prions, suggesting the existence of a general mechanism by which the appearance of prions is enhanced by heterologous prion aggregates.
朊病毒是自我传播的蛋白质构象。最近的研究对朊病毒的传播有了深入了解，但它们最初是如何出现的尚不清楚。我们之前已经确定，酵母非孟德尔性状[PIN(+)]是[PSI(+)]朊病毒从头出现所必需的。在这里，我们表明由Rnq1或Ure2形成的朊病毒的存在足以使细胞成为[PIN(+)]。因此，[PIN(+)]可能由不止一种朊病毒引起。此外，对[PIN(+)]朊病毒进行的无偏向性功能筛选发现了已知的朊病毒基因URE2、推测的朊病毒基因NEW1以及九个均携带朊病毒结构域的新型候选朊病毒基因。重要的是，Rnq1::GFP朊病毒聚集体的从头出现也需要其他朊病毒的存在，这表明存在一种普遍机制，通过该机制异源朊病毒聚集体可增强朊病毒的出现。
