用于SUMO化和小泛素样修饰物依赖性蛋白质-蛋白质相互作用的高灵敏度检测方法。
Highly sensitive assays for SUMOylation and small ubiquitin-like modifier-dependent protein-protein interactions.
作者信息
Rouleau Nathalie, Wang Jianghai, Karras Labrini, Andrews Elizabeth, Bielefeld-Sevigny Martina, Chen Yuan
机构信息
PerkinElmer BioSignal, Montreal, Quebec H3J 1R4, Canada.
出版信息
Anal Biochem. 2008 Apr 15;375(2):364-6. doi: 10.1016/j.ab.2007.11.024. Epub 2007 Nov 28.
Abstract
Small ubiquitin-like proteins (SUMO) are recently discovered post-translational modifiers that regulate protein functions and intracellular trafficking. In this study, we are describing two chemoluminescence-based assays, one for SUMOylation and another one for SUMO-mediated protein-protein interactions. These assays can be used to characterize the activity and kinetics of the enzymes that catalyze SUMOylation, and in high-throughput screening for inhibitors of SUMOylation and SUMO-dependent protein-protein interactions. These novel assays represent the most sensitive assays for ubiquitin-like systems published to date. Similar strategies can be used to develop assays for other ubiquitin-like modification systems.
摘要
小泛素样蛋白（SUMO）是最近发现的翻译后修饰因子，可调节蛋白质功能和细胞内运输。在本研究中，我们描述了两种基于化学发光的检测方法，一种用于SUMO化，另一种用于SUMO介导的蛋白质-蛋白质相互作用。这些检测方法可用于表征催化SUMO化的酶的活性和动力学，并用于高通量筛选SUMO化抑制剂和SUMO依赖性蛋白质-蛋白质相互作用。这些新检测方法是迄今为止发表的针对泛素样系统最灵敏的检测方法。类似的策略可用于开发针对其他泛素样修饰系统的检测方法。
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