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    Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13492-7. Epub 2002 Oct 7.

    Structure of the single-strand annealing domain of human RAD52 protein.

    Singleton MR, Wentzell LM, Liu Y, West SC, Wigley DB.

    Source

    Cancer Research U.K., London Research Institute, Clare Hall Laboratories, South Mimms, Hertfordshire EN6 3LD, UK.

    Abstract

    In eukaryotic cells, RAD52 protein plays a central role in genetic recombination and DNA repair by (i) promoting the annealing of complementary single-stranded DNA and (ii) stimulation of the RAD51 recombinase. The single-strand annealing domain resides in the N-terminal region of the protein and is highly conserved, whereas the nonconserved RAD51-interaction domain is located in the C-terminal region. An N-terminal fragment of human RAD52 (residues 1-209) has been purified to homogeneity and, similar to the full-size protein (residues 1-418), shown to promote single-strand annealing in vitro. We have determined the crystal structure of this single-strand annealing domain at 2.7 A. The structure reveals an undecameric (11) subunit ring with extensive subunit contacts. A large, positively charged groove runs along the surface of the ring, readily suggesting a mechanism by which RAD52 presents the single strand for reannealing with complementary single-stranded DNA.

    PMID:
    12370410
    [PubMed - indexed for MEDLINE]
    PMCID: PMC129701
    Free PMC Article

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