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In vitro role of Rad54 in Rad51-ssDNA filament-dependent homology search and synaptic complexes formation

Author

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  • Eliana Moreira Tavares

    (Genome Maintenance and Molecular Microscopy UMR8126 CNRS, Université Paris-Sud, Université Paris-Saclay, Gustave Roussy)

  • William Douglass Wright

    (University of California, Davis)

  • Wolf-Dietrich Heyer

    (University of California, Davis)

  • Eric Le Cam

    (Genome Maintenance and Molecular Microscopy UMR8126 CNRS, Université Paris-Sud, Université Paris-Saclay, Gustave Roussy)

  • Pauline Dupaigne

    (Genome Maintenance and Molecular Microscopy UMR8126 CNRS, Université Paris-Sud, Université Paris-Saclay, Gustave Roussy)

Abstract

Homologous recombination (HR) uses a homologous template to accurately repair DNA double-strand breaks and stalled replication forks to maintain genome stability. During homology search, Rad51 nucleoprotein filaments probe and interact with dsDNA, forming the synaptic complex that is stabilized on a homologous sequence. Strand intertwining leads to the formation of a displacement-loop (D-loop). In yeast, Rad54 is essential for HR in vivo and required for D-loop formation in vitro, but its exact role remains to be fully elucidated. Using electron microscopy to visualize the DNA-protein complexes, here we find that Rad54 is crucial for Rad51-mediated synaptic complex formation and homology search. The Rad54−K341R ATPase-deficient mutant protein promotes formation of synaptic complexes but not D-loops and leads to the accumulation of stable heterologous associations, suggesting that the Rad54 ATPase is involved in preventing non-productive intermediates. We propose that Rad51/Rad54 form a functional unit operating in homology search, synaptic complex and D-loop formation.

Suggested Citation

  • Eliana Moreira Tavares & William Douglass Wright & Wolf-Dietrich Heyer & Eric Le Cam & Pauline Dupaigne, 2019. "In vitro role of Rad54 in Rad51-ssDNA filament-dependent homology search and synaptic complexes formation," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-12082-z
    DOI: 10.1038/s41467-019-12082-z
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