New Method for Labeling Proteins with Fluorescent Tags
Author Information
Author(s): Charbon Godefroid, Brustad Eric, Scott Kevin A, Wang Jiangyun, Løbner-Olesen Anders, Schultz Peter G, Jacobs-Wagner Christine, Chapman Eli
Primary Institution: Yale University
Hypothesis
Can we label proteins in vivo without affecting their function using a genetically encoded fluorescent amino acid?
Conclusion
The study successfully demonstrates that a single unnatural fluorescent amino acid can be incorporated into a protein sequence without impairing its functionality.
Supporting Evidence
- The incorporation of the fluorescent amino acid did not affect the protein's ability to function in vivo.
- FtsZ10CouAA was visualized in E. coli, demonstrating the method's effectiveness.
- The study showed that FtsZ10CouAA could substitute for wild-type FtsZ in E. coli.
Takeaway
Scientists found a way to add a tiny fluorescent tag to proteins so they can see where the proteins are in living cells without messing them up.
Methodology
The study used an orthogonal tRNA/aminoacyl-tRNA synthetase pair to incorporate a fluorescent amino acid into a protein sequence in E. coli.
Limitations
The efficiency of unnatural amino acid incorporation and the photophysical properties of the fluorophore may limit the technique's application.
Digital Object Identifier (DOI)
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