Program in Chemical Biology, Memorial Sloan Kettering Cancer Center, New York, NY 10021, USA.
Program in Chemical Biology, Memorial Sloan Kettering Cancer Center, New York, NY 10021, USA; Department of Medicine, Memorial Sloan Kettering Cancer Center, New York, NY 10021, USA.
Cell Chem Biol. 2016 Jan 21;23(1):158-172. doi: 10.1016/j.chembiol.2015.12.006.
The chaperome is a large and diverse protein machinery composed of chaperone proteins and a variety of helpers, such as the co-chaperones, folding enzymes, and scaffolding and adapter proteins. Heat shock protein 90s and 70s (HSP90s and HSP70s), the most abundant chaperome members in human cells, are also the most complex. As we have learned to appreciate, their functions are context dependent and manifested through a variety of conformations that each recruit a subset of co-chaperone, scaffolding, and folding proteins and which are further diversified by the posttranslational modifications each carry, making their study through classic genetic and biochemical techniques quite a challenge. Chemical biology tools and techniques have been developed over the years to help decipher the complexities of the HSPs and this review provides an overview of such efforts with focus on HSP90 and HSP70.
伴侣蛋白组是由伴侣蛋白和各种辅助蛋白组成的一个庞大而多样的蛋白质机器，例如共伴侣蛋白、折叠酶、支架和衔接蛋白。热休克蛋白 90s 和 70s（HSP90s 和 HSP70s）是人类细胞中最丰富的伴侣蛋白组成员，也是最复杂的。正如我们逐渐认识到的那样，它们的功能取决于具体情况，并通过多种构象表现出来，每种构象都募集了一组特定的共伴侣蛋白、支架和折叠蛋白，并且通过每种蛋白携带的翻译后修饰进一步多样化，这使得通过经典的遗传和生化技术研究它们极具挑战性。多年来已经开发了化学生物学工具和技术来帮助解析 HSPs 的复杂性，本综述概述了这些努力，重点关注 HSP90 和 HSP70。
