From the Aix Marseille Univ, CNRS, Laboratoire de Bioénergétique et Ingénierie des Protéines, 13402 Marseille, France and
the Laboratory of Molecular Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892
J Biol Chem. 2019 Feb 8;294(6):2109-2120. doi: 10.1074/jbc.REV118.002806. Epub 2018 Nov 6.
Heat shock proteins 90 (Hsp90) and 70 (Hsp70) are two families of highly conserved ATP-dependent molecular chaperones that fold and remodel proteins. Both are important components of the cellular machinery involved in protein homeostasis and participate in nearly every cellular process. Although Hsp90 and Hsp70 each carry out some chaperone activities independently, they collaborate in other cellular remodeling reactions. In eukaryotes, both Hsp90 and Hsp70 function with numerous Hsp90 and Hsp70 co-chaperones. In contrast, bacterial Hsp90 and Hsp70 are less complex; Hsp90 acts independently of co-chaperones, and Hsp70 uses two co-chaperones. In this review, we focus on recent progress toward understanding the basic mechanisms of Hsp90-mediated protein remodeling and the collaboration between Hsp90 and Hsp70, with an emphasis on bacterial chaperones. We describe the structure and conformational dynamics of these chaperones and their interactions with each other and with client proteins. The physiological roles of Hsp90 in and other bacteria are also discussed. We anticipate that the information gained from exploring the mechanism of the bacterial chaperone system will provide the groundwork for understanding the more complex eukaryotic Hsp90 system and its modulation by Hsp90 co-chaperones.
热休克蛋白 90（Hsp90）和 70（Hsp70）是两个高度保守的 ATP 依赖性分子伴侣家族，它们折叠和重塑蛋白质。两者都是参与蛋白质动态平衡的细胞机制的重要组成部分，并参与几乎所有的细胞过程。尽管 Hsp90 和 Hsp70 各自独立地进行一些伴侣活性，但它们在其他细胞重塑反应中协作。在真核生物中，Hsp90 和 Hsp70 都与许多 Hsp90 和 Hsp70 共伴侣蛋白一起发挥作用。相比之下，细菌 Hsp90 和 Hsp70 则不那么复杂；Hsp90 独立于共伴侣蛋白发挥作用，而 Hsp70 使用两种共伴侣蛋白。在这篇综述中，我们重点介绍了近年来对理解 Hsp90 介导的蛋白质重塑基本机制以及 Hsp90 和 Hsp70 之间合作的研究进展，重点介绍了细菌伴侣蛋白。我们描述了这些伴侣蛋白的结构和构象动力学及其与彼此和与客户蛋白的相互作用。还讨论了 Hsp90 在 和其他细菌中的生理作用。我们预计，从探索细菌伴侣蛋白系统的机制中获得的信息将为理解更复杂的真核 Hsp90 系统及其由 Hsp90 共伴侣蛋白的调节提供基础。
