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

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 mos

SUBMITTER: Newing TP 

PROVIDER: S-EPMC9512822 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature