[URE3] prion propagation in Saccharomyces cerevisiae:: Requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p
[URE3] prion propagation in Saccharomyces cerevisiae:: Requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p
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DOI：
10.1128/mcb.20.23.8916-8922.2000
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发表时间：
2000-12-01
影响因子：
5.3
通讯作者：
Wickner, RB
中科院分区：
文献类型：
--
作者：
Moriyama, H;Edskes, HK;Wickner, RB
[URE3]非染色体遗传元件是Ure2蛋白的感染形式（朊病毒），显然是一种自我繁殖的淀粉样变性。我们发现HSP104的插入突变或缺失导致[URE3]朊病毒无法繁殖。我们的研究结果表明，热休克蛋白104是一个共同的因素，在维护两个独立的酵母朊病毒。然而，Hsp104的过量产生并不影响[URE3]的稳定性，这与[PSI+]朊病毒的稳定性相反，已知[PSI+]朊病毒通过过量产生或缺乏Hsp104而被治愈。与Hsp104一样，Hsp40类伴侣Ydj1p和Hsp70类Ssa1p可以使蛋白质复性。我们发现Ydj1p的过度产生导致[URE3]逐渐完全丧失。蛋白伴侣参与[URE3]的传播表明蛋白质构象在遗传中的作用。
The [URE3] nonchromosomal genetic element is an infectious form (prion) of the Ure2 protein, apparently a self-propagating amyloidosis. We find that an insertion mutation or deletion of HSP104 results in inability to propagate the [URE3] prion. Our results indicate that Hsp104 is a common factor in the maintenance of two independent yeast prions. However, overproduction of Hsp104 does not affect the stability of [URE3], in contrast to what is found for the [PSI+] prion, which is known to be cured by either overproduction or deficiency of Hsp104. Like Hsp104, the Hsp40 class chaperone Ydj1p, with the Hsp70 class Ssa1p, can renature proteins. We find that overproduction of Ydj1p results in a gradual complete loss of [URE3]. The involvement of protein chaperones in the propagation of [URE3] indicates a role for protein conformation in inheritance.