期刊
CHEMICAL SCIENCE
卷 9, 期 25, 页码 5551-5555出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c8sc00839f
关键词
-
资金
- National Institutes of Health [R01GM112003, R21GM126532, R01HL134780]
- Welch Foundation [BE-1913]
- American Cancer Society [RSG-16-215-01-TBE, RSG-18-043-01-LIB]
- Cancer Prevention and Research Institute of Texas [RR140053, RP170660]
- John S. Dunn Foundation
- Texas A&M University Health Science Centre Start-up Fund
- Texas A&M Triad for Transformation Program
Simple methods with straightforward readouts that enable real-time interrogation of protein quaternary structure are much needed to facilitate the physicochemical characterization of proteins at the single-cell level. After screening over a series of microtubule (MT) binders, we report herein the development of two genetically encoded tags (designated as MoTags for the monomer/oligomer detection tag) that can be conveniently fused to a given protein to probe its oligomeric state in cellulo when combined with routine fluorescence microscopy. In their monomeric form, MoTags are evenly distributed in the cytosol; whereas oligomerization enables MoTags to label MT or track MT tips in an oligomeric state-dependent manner. We demonstrate here the broad utility of engineered MoTags to aid the determination of protein oligomeric states, dissection of protein structure and function, and monitoring of protein-target interactions under physiological conditions in living cells.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据