Yeast and Fungal Prions.

Yeast and Fungal Prions.
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DOI:
10.1101/cshperspect.a023531
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发表时间:
2016-09
影响因子:
7.2
通讯作者:
R. Wickner
R. Wickner
中科院分区:
生物学1区
文献类型:
--
作者:
R. Wickner

文献摘要

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酵母和真菌朊病毒是感染性蛋白质,大多数是正常可溶性蛋白质的自繁殖淀粉样蛋白。它们的影响范围从非常轻微的损害到致命,具体影响取决于朊病毒蛋白和特定朊病毒变体(“朊病毒株”)。朊病毒淀粉样蛋白Sup 35 p、Ure 2 p和Rnq 1 p是对齐的、平行的、折叠的β-折叠,这种结构自然地暗示了蛋白质可以模板化其构象的机制,就像DNA或RNA模板化其序列一样。朊病毒的传播受到一系列伴侣系统的严重影响,最引人注目的是Hsp 104/Hsp 70/Hsp 40组合,它负责从旧丝产生新的朊病毒种子。Btn 2/Cur 1抗朊病毒系统治愈了大多数[URE 3]朊病毒,而Ssb抗朊病毒系统阻止了[PSI+]的产生。
Yeast and fungal prions are infectious proteins, most being self-propagating amyloids of normally soluble proteins. Their effects range from a very mild detriment to lethal, with specific effects dependent on the prion protein and the specific prion variant ("prion strain"). The prion amyloids of Sup35p, Ure2p, and Rnq1p are in-register, parallel, folded β-sheets, an architecture that naturally suggests a mechanism by which a protein can template its conformation, just as DNA or RNA templates its sequence. Prion propagation is critically affected by an array of chaperone systems, most notably the Hsp104/Hsp70/Hsp40 combination, which is responsible for generating new prion seeds from old filaments. The Btn2/Cur1 antiprion system cures most [URE3] prions that develop, and the Ssb antiprion system blocks [PSI+] generation.