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Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51
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RAD51AP1 is a versatile RAD51 modulator.

Lucas Kuhlen1,2, Bilge Argunhan1,2, Pengtao Liang1,2

  • 1Section of Structural and Synthetic Biology, Faculty of Medicine, Imperial College, London SW7 2AZ, United Kingdom.

Proceedings of the National Academy of Sciences of the United States of America
|December 3, 2025
PubMed
Summary
This summary is machine-generated.

RAD51AP1 stabilizes RAD51 filaments, crucial for DNA repair and telomere maintenance. This protein remodels RAD51, enhancing its DNA binding and strand exchange activity for genome stability.

Keywords:
RAD51 recombinaseRAD51AP1filaments modulationhomologous recombinationstructural biology

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cancer Biology

Background:

  • RAD51AP1 is a key factor in homologous recombination (HR) and alternative lengthening of telomeres (ALT).
  • RAD51AP1 depletion impairs HR, while its overexpression correlates with cancer malignancy.
  • The precise role of RAD51AP1 in modulating RAD51, the central HR protein, remains largely unknown.

Purpose of the Study:

  • To elucidate the hitherto unknown role of RAD51AP1 in modulating the RAD51 recombinase.
  • To reveal the structural basis of RAD51AP1-RAD51 interactions and their functional consequences.
  • To understand how RAD51AP1 influences RAD51 filament formation and DNA strand exchange.

Main Methods:

  • Biochemistry
  • Structural biology (X-ray crystallography)
  • Biophysical assays

Main Results:

  • RAD51AP1 binds to RAD51 filaments through at least three distinct RAD51-binding sites.
  • A novel binding mode stabilizes the RAD51 N-terminal domain and filament interface.
  • RAD51AP1 stabilizes RAD51-ssDNA filaments, promotes strand exchange, and enhances RAD51 oligomerization.
  • Structural data reveal conformational changes induced by RAD51AP1 binding, promoting filament nucleation and stabilization.
  • Structures of RAD51-ssDNA filaments elucidated ATP hydrolysis-dependent conformational changes and ADP's effect on DNA binding.

Conclusions:

  • RAD51AP1 acts as a versatile RAD51 modulator and filament remodeler.
  • The findings provide molecular insights into RAD51 filament dynamics and HR modulation.
  • Understanding RAD51AP1's role is critical for genome stability and cancer research.