Origins and kinetic consequences of diversity in Sup35 yeast prion fibers
Origins and kinetic consequences of diversity in Sup35 yeast prion fibers
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DOI：
10.1038/nsb786
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发表时间：
2002-05-01
期刊：
影响因子：
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通讯作者：
Weissman, JS
中科院分区：
文献类型：
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作者：
DePace, AH;Weissman, JS
朊病毒的一个显著特征是由相同朊病毒蛋白组成的感染性颗粒可以引起不同的表型。这种应变现象表明，一个单一的朊病毒蛋白可以采取多种感染性构象。在这里，我们使用了一种新的单纤维生长试验来检查由酵母Sup35朊病毒蛋白形成的淀粉样纤维的异质性。Sup35自发地形成多个，不同的和忠实地传播的纤维类型，它们在极性和总体生长速率方面都有显着差异。无论是在不同的自我传播的纤维类型的数量，以及这些差异的能力，以决定朊病毒的生长速度，这种多样性是非常适合占朊病毒株在体内观察到的表型的范围。
A remarkable feature of prions is that infectious particles composed of the same prion protein can give rise to different phenotypes. This strain phenomenon suggests that a single prion protein can adopt multiple infectious conformations. Here we use a novel single fiber growth assay to examine the heterogeneity of amyloid fibers formed by the yeast Sup35 prion protein. Sup35 spontaneously forms multiple, distinct and faithfully propagating fiber types, which differ dramatically both in their degrees of polarity and overall growth rates. Both in terms of the number of distinct self-propagating fiber types, as well as the ability of these differences to dictate the rate of prion growth, this diversity is well suited to account for the range of prion strain phenotypes observed in vivo.