1h2i Citations

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

Proc Natl Acad Sci U S A 99 13492-7 (2002)
Cited: 161 times
EuropePMC logo PMID: 12370410

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.

Reviews - 1h2i mentioned but not cited (2)

  1. Mechanism of homologous recombination and implications for aging-related deletions in mitochondrial DNA. Chen XJ. Microbiol Mol Biol Rev 77 476-496 (2013)
  2. Novel Insights into RAD52's Structure, Function, and Druggability for Synthetic Lethality and Innovative Anticancer Therapies. Balboni B, Rinaldi F, Previtali V, Ciamarone A, Girotto S, Cavalli A. Cancers (Basel) 15 1817 (2023)

Articles - 1h2i mentioned but not cited (10)



Reviews citing this publication (24)

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Articles citing this publication (125)