Some like it hot: the structure and function of small heat-shock proteins
Some like it hot: the structure and function of small heat-shock proteins
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DOI：
10.1038/nsmb993
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发表时间：
2005-10-01
影响因子：
16.8
通讯作者：
Buchner, J
中科院分区：
文献类型：
--
作者：
Haslbeck, M;Franzmann, T;Buchner, J
小分子热休克蛋白（Small heat-shock proteins，sHsps）是一类广泛存在的分子伴侣。最近的证据表明，它们通过结合非天然构象的蛋白质来维持蛋白质稳态，从而防止底物聚集。sHsp家族的一些成员在生理条件下是无活性的或仅部分活性的，并且向活性状态的转变由特定触发物（例如升高的温度）诱导。释放底物蛋白绑定到sHsps需要与ATP依赖性伴侣的合作，这表明sHsps创建一个水库的非天然蛋白质随后的重折叠。
Small heat-shock proteins (sHsps) are a widespread and diverse class of molecular chaperones. Recent evidence suggests that they maintain protein homeostasis by binding proteins in non-native conformations, thereby preventing substrate aggregation. Some members of the sHsp family are inactive or only partially active under physiological conditions, and transition toward the active state is induced by specific triggers, such as elevated temperature. Release of substrate proteins bound to sHsps requires cooperation with ATP-dependent chaperones, suggesting that sHsps create a reservoir of non-native proteins for subsequent refolding.