Exposure to high temperature or other stresses induces a synthesis of heat shock proteins. Many of these proteins are molecular chaperones, and some of them help cells to cope with heat-induced denaturation and aggregation of other proteins. In the last decade, chaperones have received increased attention in connection with their role in maintenance and propagation of the Saccharomyces cerevisiae prions, infectious or heritable agents transmitted at the protein level. Recent data suggest that functioning of the chaperones in reactivation of heat-damaged proteins and in propagation of prions is based on the same molecular mechanisms but may lead to different consequences depending on the type of aggregate. In both cases the concerted and balanced action of "chaperones' team," including Hsp104, Hsp70, Hsp40 and possibly other proteins, determines whether a misfolded protein is to be incorporated into an aggregate, rescued to the native state or targeted for degradation.

中文翻译：

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对朊病毒和非朊病毒聚集体的伴侣效应。


暴露于高温或其他压力会诱导热休克蛋白的合成。这些蛋白质中有许多是分子伴侣，其中一些帮助细胞应对热诱导的变性和其他蛋白质的聚集。在过去的十年中，伴侣蛋白因其在酿酒酵母朊病毒（在蛋白质水平上传播的传染性或遗传性病原体）的维持和繁殖中的作用而受到越来越多的关注。最近的数据表明，伴侣蛋白在热损伤蛋白质的重新激活和朊病毒的繁殖中的功能基于相同的分子机制，但根据聚集体的类型可能会导致不同的后果。在这两种情况下，“伴侣团队”（包括 Hsp104、Hsp70、Hsp40 和可能的其他蛋白质）的协调一致和平衡的行动决定了错误折叠的蛋白质是否会被整合到聚集体中、被拯救到天然状态或被靶向降解。