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Fluoride-Triggered Protein Activation via a Genetically Encoded Tyrosine Analogue.

Jieun Bae1,2, Soran Kim1, Jongdoo Choi1,2

  • 1Department of Chemistry, Pusan National University, Busan 46241, Republic of Korea.

Journal of the American Chemical Society
|November 26, 2025
PubMed
Summary

Scientists developed a new genetic tool using fluoride to control protein activity. This method allows for precise temporal regulation of biological systems in living cells and in vitro, advancing synthetic biology applications.

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Area of Science:

  • Biochemistry
  • Synthetic Biology
  • Molecular Biology

Background:

  • Fluoride can modulate biological systems.
  • Genetic encoding offers precise control over biological functions.
  • Noncanonical amino acids expand the functional repertoire of proteins.

Purpose of the Study:

  • To develop a genetically encoded actuator platform for fluoride-inducible protein control.
  • To demonstrate the site-specific incorporation of a fluoride-responsive amino acid.
  • To enable temporal regulation of protein activity in vitro and in living cells.

Main Methods:

  • Site-specific incorporation of dimethylthiophosphinoyl tyrosine (DTPY) into proteins.
  • Utilizing DTPY as a fluoride-responsive noncanonical amino acid.
  • Engineering superfolder green fluorescent protein and Cre recombinase for fluoride-dependent activity.

Main Results:

  • DTPY incorporation prevented native fluorescence in superfolder green fluorescent protein, restored by fluoride.
  • DTPY at the catalytic site of Cre recombinase enabled fluoride-induced DNA recombination.
  • Demonstrated temporal control of protein function using fluoride as a trigger.

Conclusions:

  • A versatile platform for fluoride-inducible protein control was established.
  • This method provides temporal regulation of protein activity in vitro and in vivo.
  • The approach offers a novel tool for synthetic biology and cellular engineering.