Journal
CHEMICAL SCIENCE
Volume 9, Issue 25, Pages 5551-5555Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c8sc00839f
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Funding
- 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
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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.
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