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Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51
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Two three-strand intermediates are processed during Rad51-driven DNA strand exchange.

Kentaro Ito1, Yasuto Murayama1,2,3, Masayuki Takahashi1

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Nature Structural & Molecular Biology
|January 12, 2018
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Summary

Fission yeast Rad51 protein forms distinct intermediates during DNA strand exchange. The Swi5-Sfr1 activator drives strand exchange via ATP hydrolysis, while calcium ions stabilize but do not drive the process.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Homologous recombination is crucial for DNA repair.
  • Rad51 protein forms nucleoprotein filaments with single-stranded DNA (ssDNA).
  • This filament mediates strand exchange with homologous double-stranded DNA (dsDNA).

Purpose of the Study:

  • To investigate the mechanism of strand exchange by fission yeast Rad51.
  • To elucidate the roles of Swi5-Sfr1 and calcium ions (Ca2+) in Rad51-mediated strand exchange.

Main Methods:

  • Real-time analysis of Rad51 activity.
  • Observation of DNA strand exchange intermediates.

Main Results:

  • Strand exchange proceeds through two distinct three-strand intermediates, C1 and C2.
  • C1 has an intact donor duplex, while C2 involves intertwined ssDNA and donor DNA.
  • Swi5-Sfr1 promotes the C1-C2 transition and ssDNA release, requiring ATP hydrolysis.
  • Ca2+ facilitates the C1-C2 transition but inhibits strand exchange by curbing ATP hydrolysis.

Conclusions:

  • Swi5-Sfr1 and Ca2+ exhibit different activation modes in the late synaptic phase of recombination.
  • Swi5-Sfr1 acts as a recombination activator, while Ca2+ modulates Rad51 filament activity.