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Measurement of Heme Synthesis Levels in Mammalian Cells
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Structural Basis of a Novel Heme Binding Bacterial One-Component Switch.

James J Siclari1,2, Malvin Forson1,3, Cullen Roeder1,3

  • 1Structural Biology Initiative, CUNY Advanced Science Research Center, New York, NY 10031.

Biorxiv : the Preprint Server for Biology
|April 10, 2026
PubMed
Summary

Researchers identified FG214, a novel heme-binding protein, that acts as a DNA binding switch. Redox changes trigger its transition from monomer to dimer, enabling gene regulation and potential biosensor applications.

Keywords:
Bacterial SignalingHeme Binding ProteinsOne-Component SystemsPer-ARNT-Sim domains

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Area of Science:

  • Molecular Biology
  • Protein Structure and Function
  • Biochemistry

Background:

  • One-component systems (OCSs) are crucial for rapid cellular responses to environmental stimuli.
  • Understanding sensory protein mechanisms is key to deciphering cellular adaptation.
  • FG214 is a novel putative OCS protein from *Fimbriimonas ginsengisoli*.

Purpose of the Study:

  • To characterize the novel OCS protein FG214 as a potential redox or O2-regulated transcription factor.
  • To elucidate the structural and functional mechanisms underlying FG214's activity.
  • To explore FG214's potential as a tool for gene expression regulation and biosensing.

Main Methods:

  • Spectroscopic and structural analyses (including X-ray crystallography) to determine protein conformation and heme binding.
  • In vitro DNA-binding assays to identify promoter sequences and assess ligand-enhanced binding.
  • In vivo experiments to investigate protein homodimerization.

Main Results:

  • FG214's Per-ARNT-Sim (PAS) domain binds heme b in oxidized conditions.
  • Redox changes and ligand binding induce conformational shifts, causing FG214 to transition from a monomer to a homodimer.
  • Oxidation stabilizes the helix-turn-helix (HTH)-PAS interface, while reduction or ligand binding dissociates the HTH, freeing dimerization surfaces.
  • FG214 demonstrates ligand-enhanced binding to an identified artificial promoter sequence.
  • Proof-of-concept experiments confirm FG214's ability to homodimerize in vivo.

Conclusions:

  • FG214 is a novel heme-binding PAS DNA binding protein and a potential transcription factor.
  • Its monomer-dimer transition mechanism is regulated by redox state and heme ligand binding.
  • FG214 represents a new class of heme-PAS signaling switches and shows promise for developing redox- or gas-sensitive biosensors.