Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
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DOI：
10.1016/s0092-8674(00)81223-4
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发表时间：
1998-07-10
期刊：
影响因子：
64.5
通讯作者：
Lindquist, S
中科院分区：
文献类型：
--
作者：
Glover, JR;Lindquist, S
Hsp104是一种胁迫耐受因子，通过一种未知的机制促进酵母热损伤蛋白的再激活。本文证明Hsp104直接参与了这一过程。与其他伴侣蛋白不同，Hsp104不能阻止变性蛋白的聚集。然而，与Hsp40和Hsp70协同作用，Hsp104可以重新激活已经变性并允许聚集的蛋白质，这些底物对其他伴侣蛋白的作用是不耐受的。Hsp104与存在于网织细胞裂解物中的伴侣蛋白合作，但与大肠杆菌的DnaK不合作。我们得出结论，Hsp104具有蛋白质重塑活性，可作用于被捕获的聚集蛋白，并且需要与传统伴侣蛋白特异性相互作用以促进其产生的中间体的再折叠。
Hsp104 is a stress tolerance factor that promotes the reactivation of heat-damaged proteins in yeast by an unknown mechanism. Herein, we demonstrate that Hsp104 functions in this process directly. Unlike other chaperones, Hsp104 does not prevent the aggregation of denatured proteins. However, in concert with Hsp40 and Hsp70, Hsp104 can reactivate proteins that have been denatured and allowed to aggregate, substrates refractory to the action of other chaperones. Hsp104 cooperates with the chaperones present in reticulocyte lysates but not with DnaK of E. coli. We conclude that Hsp104 has a protein remodeling activity that acts on trapped, aggregated proteins and requires specific interactions with conventional chaperones to promote refolding of the intermediates it produces.