Baker Tania A, Sauer Robert T
Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Trends Biochem Sci. 2006 Dec;31(12):647-53. doi: 10.1016/j.tibs.2006.10.006. Epub 2006 Oct 30.
ATP-powered AAA+ proteases degrade specific proteins in intracellular environments occupied by thousands of different proteins. These proteases operate as powerful molecular machines that unfold stable native proteins before degradation. Understanding how these enzymes choose the "right" protein substrates at the "right" time is key to understanding their biological function. Recently, proteomic approaches have identified numerous substrates for some bacterial enzymes and the sequence motifs responsible for recognition. Advances have also been made in elucidating the mechanism and impact of adaptor proteins in regulating substrate choice. Finally, recent biochemical dissection of the ATPase cycle and its coupling to protein unfolding has revealed fundamental operating principles of this important, ubiquitous family of molecular machines.
由ATP供能的AAA+蛋白酶在充满数千种不同蛋白质的细胞内环境中降解特定蛋白质。这些蛋白酶作为强大的分子机器，在降解之前使稳定的天然蛋白质解折叠。了解这些酶如何在“正确”的时间选择“正确”的蛋白质底物是理解其生物学功能的关键。最近，蛋白质组学方法已经确定了一些细菌酶的众多底物以及负责识别的序列基序。在阐明衔接蛋白在调节底物选择中的机制和影响方面也取得了进展。最后，最近对ATP酶循环及其与蛋白质解折叠的耦合进行的生化剖析揭示了这个重要的、普遍存在的分子机器家族的基本运作原理。
