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Updated: Jan 30, 2026

Single-Molecule Förster Resonance Energy Transfer Methods for Real-Time Investigation of the Holliday Junction Resolution by GEN1
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Junction resolving enzymes use multivalency to keep the Holliday junction dynamic.

Ruobo Zhou1,2, Olivia Yang3, Anne-Cécile Déclais4

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Holliday junction resolving enzymes maintain essential DNA dynamics after binding. This conserved mechanism allows for coordinated junction resolution, conformer exchange, and branch migration during DNA repair and recombination.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Holliday junction (HJ) resolution is critical for chromosome segregation and DNA repair.
  • HJ structural dynamics, including conformer exchange and branch migration, dictate recombination outcomes.
  • The mechanism by which enzymes achieve preferred branch points and conformers post-binding remains unclear.

Purpose of the Study:

  • To investigate the dynamics of Holliday junctions (HJs) after binding by resolving enzymes.
  • To understand how enzymes coordinate HJ resolution, conformer exchange, and branch migration.

Main Methods:

  • Single-molecule fluorescence resonance energy transfer (smFRET) analysis was employed.
  • Resolving enzymes from various species (T7 endonuclease I, RuvC, GEN1, hMus81-Eme1) were studied.

Main Results:

  • Holliday junction dynamics (conformer exchange and branch migration) persist even after enzyme binding.
  • Dimeric resolving enzymes utilize multivalent interactions, forming partially dissociated intermediates.
  • These intermediates allow the HJ to undergo largely unhindered dynamics.

Conclusions:

  • HJ resolving enzymes possess an evolutionarily conserved property enabling dynamic junction processing.
  • This mechanism provides insight into the coordination of junction resolution, conformer exchange, and branch migration.
  • Enzyme binding does not fully restrict HJ structural dynamics, which is crucial for biological outcomes.