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Updated: Jul 9, 2025

Characterizing DNA Repair Processes at Transient and Long-lasting Double-strand DNA Breaks by Immunofluorescence Microscopy
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Time-resolved crystallography captures light-driven DNA repair.

Nina-Eleni Christou1, Virginia Apostolopoulou1,2, Diogo V M Melo3

  • 1Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.

Science (New York, N.Y.)
|November 30, 2023
PubMed
Summary
This summary is machine-generated.

Photolyase uses light to repair DNA by trapping an excited flavin adenine dinucleotide (FAD) cofactor. This enzyme facilitates electron transfer to DNA, repairing damage through a novel single-bond intermediate and stepwise product release.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Photolyase is a crucial enzyme for DNA repair, utilizing light energy to reverse UV-induced damage.
  • Understanding the catalytic mechanism of photolyase is essential for comprehending DNA repair pathways.

Purpose of the Study:

  • To elucidate the reaction intermediates and mechanism of photolyase-catalyzed DNA repair.
  • To capture and characterize transient states of the enzyme during its catalytic cycle.

Main Methods:

  • Time-resolved crystallography was employed to capture short-lived intermediates.
  • Structural analysis of enzyme-cofactor-DNA complexes at different time points.

Main Results:

  • Photolyase traps the excited state of flavin adenine dinucleotide (FAD) in a bent conformation.
  • Electron transfer from excited FAD to damaged DNA initiates the repair process.
  • The DNA repair involves a single-bond intermediate, with stepwise release of thymine bases.

Conclusions:

  • The study reveals a novel mechanism for DNA repair involving a bent FAD excited state and a single-bond intermediate.
  • Stepwise product release, with the 3' thymine ejected first, is dictated by active site crowding and disrupted hydrogen bonds.