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Mechanism of homologous recombination from the RecA–ssDNA/dsDNA structures

Author

Listed:
  • Zhucheng Chen

    (Structural Biology Program,
    Cornell University Weill Medical College, New York, New York 10021, USA)

  • Haijuan Yang

    (Structural Biology Program,)

  • Nikola P. Pavletich

    (Structural Biology Program,
    Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA)

Abstract

The RecA family of ATPases mediates homologous recombination, a reaction essential for maintaining genomic integrity and for generating genetic diversity. RecA, ATP and single-stranded DNA (ssDNA) form a helical filament that binds to double-stranded DNA (dsDNA), searches for homology, and then catalyses the exchange of the complementary strand, producing a new heteroduplex. Here we have solved the crystal structures of the Escherichia coli RecA–ssDNA and RecA–heteroduplex filaments. They show that ssDNA and ATP bind to RecA–RecA interfaces cooperatively, explaining the ATP dependency of DNA binding. The ATP γ-phosphate is sensed across the RecA–RecA interface by two lysine residues that also stimulate ATP hydrolysis, providing a mechanism for DNA release. The DNA is underwound and stretched globally, but locally it adopts a B-DNA-like conformation that restricts the homology search to Watson–Crick-type base pairing. The complementary strand interacts primarily through base pairing, making heteroduplex formation strictly dependent on complementarity. The underwound, stretched filament conformation probably evolved to destabilize the donor duplex, freeing the complementary strand for homology sampling.

Suggested Citation

  • Zhucheng Chen & Haijuan Yang & Nikola P. Pavletich, 2008. "Mechanism of homologous recombination from the RecA–ssDNA/dsDNA structures," Nature, Nature, vol. 453(7194), pages 489-494, May.
    • Handle: RePEc:nat:nature:v:453:y:2008:i:7194:d:10.1038_nature06971
    DOI: 10.1038/nature06971
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    Cited by:

    1. Kamal el Battioui & Sohini Chakraborty & András Wacha & Dániel Molnár & Mayra Quemé-Peña & Imola Cs. Szigyártó & Csenge Lilla Szabó & Andrea Bodor & Kata Horváti & Gergő Gyulai & Szilvia Bősze & Judit, 2024. "In situ captured antibacterial action of membrane-incising peptide lamellae," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    2. Shih-Chi Luo & Min-Chi Yeh & Yu-Hsiang Lien & Hsin-Yi Yeh & Huei-Lun Siao & I-Ping Tu & Peter Chi & Meng-Chiao Ho, 2023. "A RAD51–ADP double filament structure unveils the mechanism of filament dynamics in homologous recombination," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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