Department of Biochemistry, McGill University, 3655 Promenade Sir William Osler, Montreal, QC H3G 1Y6, Canada.
Biochem Cell Biol. 2010 Apr;88(2):291-300. doi: 10.1139/o09-175.
Molecular chaperones of the Hsp70 family have diverse functions in cells. They assist the folding of newly synthesized and stress-denatured proteins, as well as the import of proteins into organelles, and the dissociation of aggregated proteins. The well-conserved Hsp70 chaperones are ATP dependent: binding and hydrolysis of ATP regulates their interactions with unfolded polypeptide substrates, and ATPase cycling is necessary for their function. All cellular functions of Hsp70 chaperones use the same mechanism of ATP-driven polypeptide binding and release. The Hsp40 co-chaperones stimulate ATP hydrolysis by Hsp70 and the type 1 Hsp40 proteins are conserved from Escherichia coli to humans. Various nucleotide exchange factors also promote the Hsp70 ATPase cycle. Recent advances have added to our understanding of the Hsp70 mechanism at a molecular level.
Hsp70 家族的分子伴侣在细胞中具有多种功能。它们协助新合成和应激变性的蛋白质折叠,以及蛋白质进入细胞器,以及聚集蛋白质的解离。高度保守的 Hsp70 伴侣是 ATP 依赖性的:ATP 的结合和水解调节它们与未折叠多肽底物的相互作用,并且 ATP 酶循环是其功能所必需的。Hsp70 伴侣的所有细胞功能都使用相同的机制,即 ATP 驱动的多肽结合和释放。Hsp40 共伴侣刺激 Hsp70 的 ATP 水解,并且从大肠杆菌到人类都保守了类型 1 Hsp40 蛋白。各种核苷酸交换因子也促进 Hsp70 ATP 酶循环。最近的进展增加了我们对 Hsp70 机制的分子水平的理解。