Haslbeck Martin, Franzmann Titus, Weinfurtner Daniel, Buchner Johannes
Technische Universität München, Department Chemie, Lichtenbergstr. 4, 85747 Garching, Germany.
Nat Struct Mol Biol. 2005 Oct;12(10):842-6. doi: 10.1038/nsmb993.
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.
小分子热休克蛋白（sHsps）是一类广泛存在且多样的分子伴侣。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无活性或仅部分有活性，向活性状态的转变由特定触发因素诱导，如温度升高。与结合在sHsps上的底物蛋白的释放需要与ATP依赖的伴侣蛋白协同作用，这表明sHsps形成了一个非天然蛋白质库以供后续重新折叠。
