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Redβ177 annealase structure reveals details of oligomerization and λ Red-mediated homologous DNA recombination

Author

Listed:
  • Timothy P. Newing

    (University of Wollongong
    Illawarra Health and Medical Research Institute)

  • Jodi L. Brewster

    (University of Wollongong
    Illawarra Health and Medical Research Institute
    ARC Centre for Cryo-electron Microscopy of Membrane Proteins, University of Wollongong)

  • Lucy J. Fitschen

    (University of Wollongong
    Illawarra Health and Medical Research Institute
    ARC Centre for Cryo-electron Microscopy of Membrane Proteins, University of Wollongong)

  • James C. Bouwer

    (University of Wollongong
    ARC Centre for Cryo-electron Microscopy of Membrane Proteins, University of Wollongong)

  • Nikolas P. Johnston

    (University of Wollongong)

  • Haibo Yu

    (University of Wollongong
    Illawarra Health and Medical Research Institute)

  • Gökhan Tolun

    (University of Wollongong
    Illawarra Health and Medical Research Institute
    ARC Centre for Cryo-electron Microscopy of Membrane Proteins, University of Wollongong)

Abstract

The Redβ protein of the bacteriophage λ red recombination system is a model annealase which catalyzes single-strand annealing homologous DNA recombination. Here we present the structure of a helical oligomeric annealing intermediate of Redβ, consisting of N-terminal residues 1-177 bound to two complementary 27mer oligonucleotides, determined via cryogenic electron microscopy (cryo-EM) to a final resolution of 3.3 Å. The structure reveals a continuous binding groove which positions and stabilizes complementary DNA strands in a planar orientation to facilitate base pairing via a network of hydrogen bonding. Definition of the inter-subunit interface provides a structural basis for the propensity of Redβ to oligomerize into functionally significant long helical filaments, a trait shared by most annealases. Our cryo-EM structure and molecular dynamics simulations suggest that residues 133-138 form a flexible loop which modulates access to the binding groove. More than half a century after its discovery, this combination of structural and computational observations has allowed us to propose molecular mechanisms for the actions of the model annealase Redβ, a defining member of the Redβ/RecT protein family.

Suggested Citation

  • Timothy P. Newing & Jodi L. Brewster & Lucy J. Fitschen & James C. Bouwer & Nikolas P. Johnston & Haibo Yu & Gökhan Tolun, 2022. "Redβ177 annealase structure reveals details of oligomerization and λ Red-mediated homologous DNA recombination," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
  • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-33090-6
    DOI: 10.1038/s41467-022-33090-6
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    Cited by:

    1. Brian J. Caldwell & Andrew S. Norris & Caroline F. Karbowski & Alyssa M. Wiegand & Vicki H. Wysocki & Charles E. Bell, 2022. "Structure of a RecT/Redβ family recombinase in complex with a duplex intermediate of DNA annealing," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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