Department of Biological Chemistry and Molecular Pharmacology , Harvard Medical School , Boston , Massachusetts 02115 , United States.
Biochemistry. 2019 May 21;58(20):2509-2518. doi: 10.1021/acs.biochem.9b00106. Epub 2019 Apr 12.
Regulated proteolysis of signaling proteins under mechanical tension enables cells to communicate with their environment in a variety of developmental and physiologic contexts. The role of force in inducing proteolytic sensitivity has been explored using magnetic tweezers at the single-molecule level with bead-tethered assays, but such efforts have been limited by challenges in ensuring that beads not be restrained by multiple tethers. Here, we describe a multiplexed assay for single-molecule proteolysis that overcomes the multiple-tether problem using a flow-extension strategy on a microscope equipped with magnetic tweezers. Particle tracking and computational sorting of flow-induced displacements allow assignment of tethered substrates to singly captured and multiply tethered bins, with the fraction of fully mobile, single-tether substrates depending inversely on the concentration of substrate loaded on the coverslip. Computational exclusion of multiple-tether beads enables robust assessment of on-target proteolysis by the highly specific tobacco etch virus protease and the more promiscuous metalloprotease ADAM17. This method should be generally applicable to a wide range of proteases and readily extensible to robust evaluation of proteolytic sensitivity as a function of applied magnetic force.
在机械张力下,对信号蛋白的调控性蛋白水解使细胞能够在多种发育和生理环境下与环境进行交流。使用磁镊在带有珠状连接物的测定中,在单分子水平上探索了力在诱导蛋白水解敏感性方面的作用,但这些努力受到了确保珠子不会被多个连接物限制的挑战的限制。在这里,我们描述了一种用于单分子蛋白水解的多重分析方法,该方法使用配备有磁镊的显微镜上的流延策略克服了多连接问题。颗粒跟踪和流动诱导位移的计算排序允许将连接的底物分配到单个捕获和多个连接的容器中,完全可移动的单连接底物的分数与盖玻片上加载的底物浓度成反比。通过高度特异性的烟草蚀纹病毒蛋白酶和更混杂的金属蛋白酶 ADAM17 对多个连接珠的计算排除,可实现对靶蛋白水解的稳健评估。该方法应广泛适用于多种蛋白酶,并易于扩展,以稳健评估作为施加磁场的函数的蛋白水解敏感性。