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

Timothy P. Newing, Jodi L. Brewster, Lucy J. Fitschen, James C. Bouwer, Nikolas P. Johnston, Haibo Yu and Gökhan Tolun ()
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Timothy P. Newing: University of Wollongong
Jodi L. Brewster: University of Wollongong
Lucy J. Fitschen: University of Wollongong
James C. Bouwer: University of Wollongong
Nikolas P. Johnston: University of Wollongong
Haibo Yu: University of Wollongong
Gökhan Tolun: University of Wollongong

Nature Communications, 2022, vol. 13, issue 1, 1-14

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-33090-6

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