ArticleProceedings of the National Academy of Sciences of the United States of America2002
Structure of the single-strand annealing domain of human RAD52 protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 148 papers.
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148 citing papers in PubMed, 230 citations in OpenAlex.
- Mechanism of single-strand annealing from native mass spectrometry and cryo-EM structures of RAD52 homolog Mgm101.Nucleic acids research · 2026Article
- Mutations altering the DNA binding domains of the human RAD52 protein exert distinct effects on homologous recombination repair in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2026Article
- The human RAD52 complex undergoes phase separation and facilitates bundling and end-to-end tethering of RAD51 presynaptic filaments.Nucleic acids research · 2026Article
- RAD52's active form is not a ring.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Monomers and short oligomers of human RAD52 promote single-strand annealing.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Phage parasites targeting phage homologous recombinases provide antiviral immunity.Nature communications · 2025Article
- Transcriptomics and Proteomics Analysis of the Liver ofInternational journal of molecular sciences · 2025Article
- A structural phylogenetic tree of Rad52 and its annealase superfamily.Computational and structural biotechnology journal · 2025Article
- Homologous Recombination and DNA Intermediates Analyzed by Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2025Article
- The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction.iScience · 2024Article
- The human RAD52 complex undergoes phase separation and facilitates bundling and end-to-end tethering of RAD51 presynaptic filaments.bioRxiv : the preprint server for biology · 2024Article
- A glimpse into the hidden world of the flexible C-terminal protein binding domains of human RAD52.Journal of structural biology · 2024Article
- An integrative structural study of the human full-length RAD52 at 2.2 Å resolution.Communications biology · 2024Article
- The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction.bioRxiv : the preprint server for biology · 2024Article
- Article
- Human RAD52 stimulates the RAD51-mediated homology search.Life science alliance · 2024Article
- Half a century after their discovery: Structural insights into exonuclease and annealase proteins catalyzing recombineering.Engineering microbiology · 2024Review
- Yeast Rad52 is a homodecamer and possesses BRCA2-like bipartite Rad51 binding modes.Nature communications · 2023Article
- FIRRM cooperates with FIGNL1 to promote RAD51 disassembly during DNA repair.Science advances · 2023Article
88 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.