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Structure of the single-strand annealing domain of human RAD52 protein
Open accessAbstract
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 Å. 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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Cited by
Genetic Steps of Mammalian Homologous Repair with Distinct Mutagenic Consequences
Stark, J. M., Pierce, A. J., Oh, J., Pastink, A., & Jasin, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.21.9305-9316.2004 · Cited by 501
Human Fanconi anemia monoubiquitination pathway promotes homologous DNA repair
Nakanishi, K., Yang, Y.-G., Pierce, A. J., Taniguchi, T., Digweed, M., D'Andrea, A. D., Wang, Z.-Q., & Jasin, M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407796102 · Cited by 384
Mutational signatures reveal the role of RAD52 in p53-independent p21-driven genomic instability
Galanos, P., Pappas, G., Polyzos, A., Kotsinas, A., Svolaki, I., Giakoumakis, N. N., Glytsou, C., Pateras, I. S., Swain, U., Souliotis, V. L., et al. (2018) · Genome Biology · doi:10.1186/s13059-018-1401-9 · Cited by 67
Newing, T. P., Brewster, J. L., Fitschen, L. J., Bouwer, J. C., Johnston, N. P., Yu, H., & Tolun, G. (2022) · Nature Communications · doi:10.1038/s41467-022-33090-6 · Cited by 22
A structural phylogenetic tree of Rad52 and its annealase superfamily
Al-Fatlawi, A., Hossen, M. B., de Paula Lopes, S., Stewart, A. F., & Schroeder, M. (2025) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2024.12.012 · Cited by 3
Metadata
- Authors
- Singleton, M. R., Wentzell, L. M., Liu, Y., West, S. C., & Wigley, D. B.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2002-10-07
- Volume
- 99
- Issue
- 21
- Pages
- 13492-13497
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2060710645
- Cited by
- 222
- References
- 0
- FWCI
- 3.89
- Type
- journal article
- Language
- en
- Open access
- green
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- Singleton, M. R., Wentzell, L. M., Liu, Y., West, S. C., & Wigley, D. B. (2002). Structure of the single-strand annealing domain of human RAD52 protein. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.212449899
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