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The basic reaction of homologous recombination (HR) involves two chromatids that contain DNA sequences sharing a significant stretch of identity. One of these sequences uses a strand from another as a template to synthesize DNA in an enzyme-catalyzed reaction. The final product is a novel amalgamation of the two substrates. To ensure an accurate recombination of sequences, HR is restricted to the S and G2 phases of the cell cycle. At these stages, the DNA has been replicated already and the...
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Related Experiment Video

Updated: Sep 11, 2025

Detection of Homologous Recombination Intermediates via Proximity Ligation and Quantitative PCR in Saccharomyces cerevisiae
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Structure guided functional analysis of the S. cerevisiae Mre11 complex

Marcel Hohl1, You Yu2,3,4, Vitaly Kuryavyi5

  • 1Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY, USA.

Nature Communications
|August 12, 2025
PubMed
Summary

The Mre11-Rad50 complex

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • The Mre11 complex (Mre11, Rad50, Nbs1) is crucial for eukaryotic DNA damage response.
  • It detects and repairs DNA double-strand breaks (DSBs) and activates signaling pathways.
  • Mre11 and Rad50 are conserved core components, while Nbs1 is eukaryotic-specific.

Purpose of the Study:

  • To determine the cryo-EM structure of the Saccharomyces cerevisiae Mre11-Rad50 complex bound to dsDNA.
  • To investigate protein interfaces and DNA binding properties through mutational analysis.
  • To understand the role of the Rad50 coiled-coil domain in ATP hydrolysis.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) at 3.2 Å resolution.
  • Detailed mutational analyses of protein interfaces.
  • Biochemical assays to assess DNA binding and ATP hydrolysis.

Main Results:

  • A high-resolution cryo-EM structure of the Mre11-Rad50-dsDNA complex was obtained.
  • Conserved residues critical for complex assembly and DNA binding were identified in Mre11 and Rad50.
  • The Rad50 coiled-coil domain was shown to influence ATP hydrolysis over long distances.

Conclusions:

  • The study provides structural insights into the Mre11-Rad50 complex's function in DNA repair.
  • Identified key residues are essential for complex integrity and DNA interaction.
  • Structural and functional data elucidate the mechanism of DNA damage signaling and repair.