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The C-terminal Helices of Heat Shock Protein 70 Are Essential for J-domain Binding and ATPase Activation*

renchunxiao 添加于 2012/2/21 15:50:02  974次阅读 | 0次推荐 | 0个评论

The J-domain co-chaperones work together with the heat shock protein 70 (HSP70) chaperone to regulate many cellular events, but the mechanism underlying the J-domain-mediated HSP70 function remains elusive. We studied the interaction between human-inducible HSP70 and Homo sapiens J-domain protein (HSJ1a), a J domain and UIM motif-containing co-chaperone. The J domain of HSJ1a shares a conserved structure with other J domains from both eukaryotic and prokaryotic species, and it mediates the interaction with and the ATPase cycle of HSP70. Our in vitro study corroborates that the N terminus of HSP70 including the ATPase domain and the substrate-binding β-subdomain is not sufficient to bind with the J domain of HSJ1a. The C-terminal helical α-subdomain of HSP70, which was considered to function as a lid of the substrate-binding domain, is crucial for binding with the J domain of HSJ1a and stimulating the ATPase activity of HSP70. These fluctuating helices are likely to contribute to a proper conformation of HSP70 for J-domain binding other than directly bind with the J domain. Our findings provide an alternative mechanism of allosteric activation for functional regulation of HSP70 by its J-domain co-chaperones.

作 者:Xue-Chao Gao‡, Chen-Jie Zhou‡, Zi-Ren Zhou‡, Meng Wu‡, Chun-Yang Cao§ and Hong-Yu Hu‡,1
期刊名称: JBC
期卷页: 第卷 第期 页
学科领域:生命科学 » 生物物理、生物化学与分子生物学 » 生物大分子结构与功能
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原文链接:http://www.jbc.org/content/287/8/6044.abstract
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相关报道: http://paper.sciencenet.cn/htmlpaper/20122211556364622494.shtm
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