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Related Experiment Video

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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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A bioorthogonal small-molecule-switch system for controlling protein function in live cells.

Peng Liu1, Abram Calderon, Georgios Konstantinidis

  • 1Chemical Genomics Centre of the Max Planck Society, Otto-Hahn-Str. 15, 44227 Dortmund (Germany) http://www.cgc.mpg.de/index.php/research-groups/rg-dr-yaowen-wu/research; Abteilung Physikalische Biochemie, Max-Planck-Institut für molekulare Physiologie, Otto-Hahn-Str. 11, 44227, Dortmund (Germany).

Angewandte Chemie (International Ed. in English)
|July 29, 2014
PubMed
Summary

This study introduces a novel, rapidly reversible chemically induced dimerization (CID) system. The new bioorthogonal system uses a synthetic ligand of FKBP

Keywords:
cell protrusiondimerizationfluorescenceintracellular translocationproteins

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Synthetic Biology

Background:

  • Chemically induced dimerization (CID) is vital for controlling protein interactions.
  • Traditional dimerizers like rapamycin have limitations, including slow reversibility and off-target binding in vivo.
  • A need exists for more precise and rapidly reversible CID systems for biological research.

Purpose of the Study:

  • To develop a novel bioorthogonal system for rapid and reversible chemically induced dimerization (CID).
  • To create a new dimerizer molecule for precise control of protein-protein interactions in vivo.

Main Methods:

  • A novel dimerizer, synthetic ligand of FKBP' (SLF') linked to trimethoprim (TMP), was synthesized.
  • The system utilizes the F36V mutant of FK506-binding protein (FKBP) and E. coli dihydrofolate reductase (eDHFR).
  • Heterodimerization was induced by the SLF'-TMP dimerizer and disrupted by TMP alone.

Main Results:

  • The SLF'-TMP system achieved rapid and reversible heterodimerization of FKBP(F36V) and eDHFR with a dissociation constant of 0.12 μM.
  • Addition of trimethoprim (TMP) alone was sufficient to rapidly dissociate the induced heterodimers.
  • The system demonstrated successful application in controlling protein function in vivo.

Conclusions:

  • The developed bioorthogonal CID system offers rapid reversibility and precise control over protein interactions.
  • This novel system serves as an invaluable tool for modulating protein function in vivo.
  • The system has broad applicability for researchers needing to control protein activity dynamically.