Wickner Sue, Nguyen Thu-Lan Lily, Genest Olivier
Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA; email:
Current affiliation: Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.
Annu Rev Microbiol. 2021 Oct 8;75:719-739. doi: 10.1146/annurev-micro-032421-035644. Epub 2021 Aug 10.
Heat shock protein 90 (Hsp90) is a molecular chaperone that folds and remodels proteins, thereby regulating the activity of numerous substrate proteins. Hsp90 is widely conserved across species and is essential in all eukaryotes and in some bacteria under stress conditions. To facilitate protein remodeling, bacterial Hsp90 collaborates with the Hsp70 molecular chaperone and its cochaperones. In contrast, the mechanism of protein remodeling performed by eukaryotic Hsp90 is more complex, involving more than 20 Hsp90 cochaperones in addition to Hsp70 and its cochaperones. In this review, we focus on recent progress toward understanding the basic mechanisms of bacterial Hsp90-mediated protein remodeling and the collaboration between Hsp90 and Hsp70. We describe the universally conserved structure and conformational dynamics of these chaperones and their interactions with one another 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 a framework for understanding the more complex eukaryotic Hsp90 system.
热休克蛋白90（Hsp90）是一种分子伴侣，可折叠并重塑蛋白质，从而调节众多底物蛋白的活性。Hsp90在物种间广泛保守，在所有真核生物以及某些处于应激条件下的细菌中都至关重要。为促进蛋白质重塑，细菌Hsp90与Hsp70分子伴侣及其共伴侣协同作用。相比之下，真核生物Hsp90进行蛋白质重塑的机制更为复杂，除了Hsp70及其共伴侣外，还涉及20多种Hsp90共伴侣。在这篇综述中，我们重点关注在理解细菌Hsp90介导的蛋白质重塑基本机制以及Hsp90与Hsp70之间协同作用方面的最新进展。我们描述了这些伴侣蛋白普遍保守的结构和构象动力学，以及它们彼此之间以及与客户蛋白的相互作用。还讨论了Hsp90在细菌和其他细菌中的生理作用。我们预计，从探索细菌伴侣系统机制中获得的信息将为理解更复杂的真核生物Hsp90系统提供一个框架。
