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A F420-dependent Single Domain Chemogenetic Tool for Protein De-dimerization.

James Antoney1, Stephanie Kainrath2, Joshua G Dubowsky3

  • 1Research School of Chemistry, Australian National University, 137 Sullivans Creek Road, Canberra 2601 ACT, Australia; ARC Centre of Excellence in Synthetic Biology, Research School of Chemistry, Australian National University, 137 Sullivans Creek Road, Canberra 2601 ACT, Australia.

Journal of Molecular Biology
|May 5, 2025
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel chemogenetic tool using a mycobacterial protein (MSMEG_2027) that dissociates upon binding its native cofactor F420. This F420-dependent de-homodimerization switch enables controlled protein complex regulation in human cells.

Keywords:
bioorthogonaldimerizationoxidoreductaseprotein-protein interactionreceptor tyrosine kinase

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Protein-protein interactions (PPIs) are crucial for cellular functions.
  • Chemogenetic tools controlling PPIs are valuable for research and clinical applications.
  • Existing methods primarily induce protein association, with limited options for dissociation.

Purpose of the Study:

  • To develop a novel bioorthogonal chemogenetic tool for controlled protein complex dissociation.
  • To exploit the F420-dependent dissociation of mycobacterial MSMEG_2027 as a monomerization switch.
  • To demonstrate the tool's utility in regulating signaling pathways in human cells.

Main Methods:

  • X-ray crystallography to determine the structure of MSMEG_2027 and its interaction with F420.
  • Fusion of MSMEG_2027 to a chimeric fibroblast growth factor receptor 1 (FGFR1) tyrosine kinase.
  • Application in human cells to modulate MAPK/ERK signaling.

Main Results:

  • MSMEG_2027 forms a unique domain-swapped dimer that dissociates upon F420 binding.
  • F420 binding induces N-terminal helix rearrangement, leading to dimer dissolution.
  • The tool successfully induced and released MAPK/ERK signaling downstream of FGFR1 in human cells.

Conclusions:

  • MSMEG_2027 serves as a novel, F420-dependent chemogenetic de-homodimerization switch.
  • This single-domain tool offers a stoichiometric and bioorthogonal mechanism for controlling protein complexes in situ.
  • The approach provides a new avenue for investigating protein interactions within living systems.