Activation of the ATPase activity of Hsp90 by the stress-regulated cochaperone Aha1
Activation of the ATPase activity of Hsp90 by the stress-regulated cochaperone Aha1
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DOI：
10.1016/s1097-2765(02)00785-2
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发表时间：
2002-12-01
期刊：
影响因子：
16
通讯作者：
Prodromou, C
中科院分区：
文献类型：
--
作者：
Panaretou, B;Siligardi, G;Prodromou, C
Hsp 90对客户蛋白的激活涉及大量的辅助分子伴侣，这些辅助分子伴侣的作用尚不清楚。已经鉴定了一个普遍存在的应激调节蛋白家族（Aha 1，Hsp 90 ATP酶的激活剂），其直接结合Hsp 90，并且是体内Hsp 90依赖性激活客户如v-Src所需的，暗示它们是Hsp 90系统的辅伴侣。在体外，Aha 1和其较短的同源物，Hch 1，刺激固有的ATP酶活性的酵母和人类热休克蛋白90。这些热休克蛋白90辅伴侣蛋白激活剂的鉴定增加了辅伴侣蛋白在调节热休克蛋白90伴侣蛋白循环的ATP酶偶联构象变化中的复杂作用。
Client protein activation by Hsp90 involves a plethora of cochaperones whose roles are poorly defined. A ubiquitous family of stress-regulated proteins have been identified (Aha1, activator of Hsp90 ATPase) that bind directly to Hsp90 and are required for the in vivo Hsp90-dependent activation of clients such as v-Src, implicating them as cochaperones of the Hsp90 system. In vitro, Aha1 and its shorter homolog, Hch1, stimulate the inherent ATPase activity of yeast and human Hsp90. The identification of these Hsp90 cochaperone activators adds to the complex roles of cochaperones in regulating the ATPase-coupled conformational changes of the Hsp90 chaperone cycle.