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首页> 外文期刊>EMBO Journal >Molecular chaperones and the assembly of the prion Sup35p, an in vitro study
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Molecular chaperones and the assembly of the prion Sup35p, an in vitro study

机译：分子伴侣’和朊病毒的组装Sup35p,体外研究

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摘要

The protein Sup35 from Saccharomyces cerevisiae possesses prion properties. In vivo, a high molecular weight form of Sup35p is associated to the [ PSI (+)] factor. The continued propagation of [ PSI (+)] is highly dependent on the expression levels of molecular chaperones from the Hsp100, 70 and 40 families; however, so far, their role in this process is unclear. We have developed a reproducible in vitro system to study the effects of molecular chaperones on the assembly of full- length Sup35p. We show that Hsp104p greatly stimulates the assembly of Sup35p into fibrils, whereas Ydj1p has inhibitory effect. Hsp82p, Ssa1p and Sis1p, individually, do not affect assembly. In contrast, Ssa1p together with either of its Hsp40 cochaperones blocks Sup35p polymerization. Furthermore, Ssa1p and Ydj1p or Sis1p can counteract the stimulatory activity of Hsp104p, by forming complexes with Sup35p oligomers, in an ATP- dependent manner. Our observations reveal the functional differences between Hsp104p and the Hsp70 - 40 systems in the assembly of Sup35p into fibrils and bring new insight into the mechanism by which molecular chaperones influence the propagation of [ PSI (+)].
机译：酿酒酵母的蛋白质Sup35拥有朊病毒属性。分子量Sup35p形式相关联(ψ(+))的因素。PSI(+)的高度依赖表达水平的分子伴侣’Hsp100 70和40个家庭;在这个过程中所扮演的角色还不清楚。开发了一种可再生的体外系统来研究分子伴侣’的的影响完整的组装——Sup35p长度。Hsp104p大大刺激Sup35p的组装成纤维,而Ydj1p抑制的效果。不影响组装。与它的Hsp40 cochaperones块Sup35p聚合。Ydj1p或Sis1p可以抵消刺激Hsp104p活动,形成复合物Sup35p寡聚物,ATP -依赖的方式。我们的观察揭示的功能Hsp104p和Hsp70 - 40之间的区别系统在组装Sup35p成纤维并将新的见解的机制分子伴侣’影响的传播

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