What question did this study set out to answer?

Determine the atomic structure of the conserved single-strand annealing domain of human RAD52 to elucidate its mechanism in DNA recombination and repair.

October 7, 2002Proceedings of the National Academy of Sciences

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

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Authors

MSMartin R. SingletonUniversity of Edinburgh LWLois M. WentzellCancer Research UK YLYilun LiuJilin University

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Implication

Structural analysis reveals an eleven-subunit ring in the human RAD52 domain, suggesting a mechanism for presenting single-stranded DNA during repair.

Key Points

Determine the atomic structure of the conserved single-strand annealing domain of human RAD52 to elucidate its mechanism in DNA recombination and repair.
Purified an N-terminal fragment of human RAD52 (residues 1–209) to homogeneity.
Demonstrated in vitro single-strand annealing activity comparable to the full-length protein (residues 1–418).
Solved the three-dimensional crystal structure of the domain at 2.7 Å resolution.
The single-strand annealing domain forms an undecameric (11-subunit) ring architecture mediated by extensive inter-subunit contacts.
A large, positively charged groove spans the surface of the ring, establishing the structural basis for presenting single-stranded DNA for reannealing with complementary strands.

Cite This Study

Singleton et al. (2002) studied this question.

synapsesocial.com/papers/6a94d3cd5c8f1b54a2168b17 https://doi.org/10.1073/pnas.212449899

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Implication

Structural analysis reveals an eleven-subunit ring in the human RAD52 domain, suggesting a mechanism for presenting single-stranded DNA during repair.

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

Discussion

Member takes

Implication

Key Points

Cite This Study

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

Discussion

Member takes

Implication

Key Points

Cite This Study

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