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BCDX2-CX3 and DX2-CX3 complexes assemble and stabilize RAD51 filaments.

Christopher W Koo1, Jiaqi Xiao1, Sebastien Coassolo2

  • 1Protein Sciences, Genentech Inc., South San Francisco, CA, USA.

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|March 2, 2026
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Summary
This summary is machine-generated.

Five RAD51 paralogs, crucial for DNA repair and preventing cancer, form a supercomplex. This complex acts as a DNA repair "loader" and "anchor," clarifying their roles in genomic integrity.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Homologous recombination (HR) repairs DNA double-strand breaks, maintaining genomic integrity.
  • RAD51 paralogs (RAD51B, RAD51C, RAD51D, XRCC2, XRCC3) regulate RAD51 recombinase assembly, crucial for HR.
  • Dysregulation of HR and RAD51 paralogs is linked to cancer and genetic disorders.

Purpose of the Study:

  • To elucidate the assembly and function of the five human RAD51 paralogs in DNA repair.
  • To determine the structural architecture of RAD51 paralog complexes bound to single-stranded DNA (ssDNA).
  • To define the distinct roles of RAD51 paralog complexes in the homologous recombination pathway.

Main Methods:

  • Biochemical assays to study complex formation and ATPase activity.
  • Single-stranded DNA (ssDNA) binding studies.
  • Structural analysis of RAD51 paralog assemblies.

Main Results:

  • All five RAD51 paralogs assemble into a single ATP-dependent supercomplex (BCDX2-CX3-RAD51) on ssDNA.
  • A RAD51B-independent DX2-CX3 complex (RAD51D-XRCC2-RAD51C-XRCC3) acts as a stable RAD51 anchor.
  • Distinct functional modules, a dynamic 'loader' (BCDX2-CX3) and a stable 'anchor' (DX2-CX3), were identified.

Conclusions:

  • A unifying mechanism for human RAD51 paralog function in HR is proposed.
  • The identified supercomplex architecture provides a template for RAD51 filament formation.
  • This research offers an atomic framework for understanding cancer-associated mutations in RAD51 paralogs.