Multiple effects of trehalose on protein folding in vitro and in vivo
Multiple effects of trehalose on protein folding in vitro and in vivo
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DOI：
10.1016/s1097-2765(00)80064-7
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发表时间：
1998-04-01
期刊：
影响因子：
16
通讯作者：
Lindquist, S
中科院分区：
文献类型：
--
作者：
Singer, MA;Lindquist, S
海藻糖是由不同的生物体在不同的逆境中大量产生的。海藻糖在体外可防止蛋白质在高温下变性，但其在体内耐受应激中的作用存在争议。我们报道了海藻糖在热休克期间稳定酵母细胞中的蛋白质。令人惊讶的是，海藻糖还抑制变性蛋白质的聚集，使它们保持在部分折叠的状态，分子伴侣可以重新激活它们。然而，海藻糖的持续存在干扰了折叠，这表明为什么海藻糖在热休克后会迅速水解。这些发现协调了关于海藻糖在胁迫耐受性中的作用的相互矛盾的报道，为获得蛋白质折叠中间体提供了一种新的工具，并定义了调节应激耐受性和蛋白质聚集的新参数。
The disaccharide trehalose is produced in large quantities by diverse organisms during a variety of stresses. Trehalose prevents proteins from denaturing at high temperatures in vitro, but its function in stress tolerance in vivo is controversial. We report that trehalose stabilizes proteins in yeast cells during heat shock. Surprisingly, trehalose also suppresses the aggregation of denatured proteins, maintaining them in a partially-folded state from which they can be reactivated by molecular chaperones. The continued presence of trehalose, however, interferes with refolding, suggesting why it is rapidly hydrolyzed following heat shock. These findings reconcile conflicting reports on the role of trehalose in stress tolerance, provide a novel tool for accessing protein folding intermediates, and define new parameters for modulating stress tolerance and protein aggregation.