Zhou Jiaqi, Li Xinran, Wen Qing, Gan Haiyun
Guangdong Provincial Key Laboratory of Synthetic Genomics, Key Laboratory of Quantitative Synthetic Biology, Shenzhen Institute of Synthetic Biology, Shenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen, China.
Methods Mol Biol. 2025;2953:295-310. doi: 10.1007/978-1-0716-4694-6_19.
Exploring protein interactions is essential for understanding cellular biological processes. Traditional methods for studying protein-protein interactions often face limitations in capturing transient or low-affinity interactions due to harsh lysis conditions or antibody specificity challenges. Proximity labeling has emerged as a robust technique that utilizes engineered enzymes to covalently tag proximal proteins, preserving their interactions in vivo. This chapter introduces an advanced method called antibody-mediated protein A-APEX2 labeling (AMAPEX), which enhances the established APEX2 system. AMAPEX utilizes specific antibodies to tether a modified protein to a protein A-APEX2 fusion, enabling targeted biotin labeling of proximal proteins. These labeled proteins are subsequently isolated using streptavidin beads and analyzed by mass spectrometry. Validation of the method is demonstrated by profiling histone modification proxeomes, demonstrating its accuracy in identifying associated cellular components. AMAPEX represents a significant advancement in mapping protein interactions, particularly in the context of posttranslational modifications, making it a valuable tool for biological research and therapeutic development.
探索蛋白质相互作用对于理解细胞生物学过程至关重要。传统的研究蛋白质-蛋白质相互作用的方法,由于苛刻的裂解条件或抗体特异性挑战,在捕获瞬时或低亲和力相互作用方面常常面临局限性。邻近标记已成为一种强大的技术,它利用工程酶对近端蛋白质进行共价标记,在体内保留它们的相互作用。本章介绍了一种称为抗体介导的蛋白A-APEX2标记(AMAPEX)的先进方法,该方法改进了已有的APEX2系统。AMAPEX利用特异性抗体将修饰蛋白与蛋白A-APEX2融合体连接起来,实现对近端蛋白质的靶向生物素标记。随后使用链霉亲和素磁珠分离这些标记的蛋白质,并通过质谱进行分析。通过对组蛋白修饰近端组进行分析,证明了该方法的有效性,展示了其在识别相关细胞成分方面的准确性。AMAPEX在绘制蛋白质相互作用图谱方面取得了重大进展,特别是在翻译后修饰的背景下,使其成为生物学研究和治疗开发的宝贵工具。