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Gene Review

RAD52  -  RAD52 homolog (S. cerevisiae)

Homo sapiens

Synonyms: DNA repair protein RAD52 homolog
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Disease relevance of RAD52

  • Two premature stop codons, Ser346ter and Tyr415ter, were identified in germ-line RAD52 alleles from 5% of early-onset breast cancer cases [1].
  • When probed with hydroxyl radicals, ssDNA-RAD52 complexes exhibit a four-nucleotide repeat hypersensitivity pattern [2].
  • The RAD52 gene is involved in the homologous recombination repair pathway and is a plausible candidate ovarian cancer predisposition gene [3].
  • Escherichia coli RecO and SSB proteins, which are functional homologues of Rad52 and RPA, also facilitated the same reaction, demonstrating its conserved nature [4].
  • Reverse transcription-PCR analysis of cultured human diploid fibroblasts, as well as fibrosarcoma cells, revealed that while hRAD52 is expressed at low, but detectable levels in these cells, the pseudogene is not [5].

High impact information on RAD52

  • AID-dependent generation of resected double-strand DNA breaks and recruitment of Rad52/Rad51 in somatic hypermutation [6].
  • Thus, resistance to melphalan may require accelerated DNA repair by either recombinational repair mechanisms involving Rad51-related proteins (including x-ray repair cross-complementing proteins Xrcc2, Xrcc3, and Rad52) or by nonhomologous endjoining involving DNA-dependent protein kinase (DNA-PK) and Ku proteins [7].
  • Increased retroviral integration is the first major phenotype described for a RAD52 deficiency in mammalian cells [8].
  • Instead, the mechanism of attenuation of retroviral infection by RAD52 appears to be based upon competition between the RAD52 protein and active integration complexes for the retroviral cDNA genome [8].
  • Overexpression of Rad52 prevented endoreduplication in RPA-overexpressing cells, in XRCC3(-/-) cells and in the variant-expressing cells, suggesting that deregulated RPA was responsible for the increased endoreduplication [9].

Biological context of RAD52

  • The presence of common nonsense mutations in RAD52 within the population may have significance for other conditions associated with potential alterations in DNA damage repair pathways [1].
  • Fluorescence resonance energy transfer (FRET) analyses show that WRN and RAD52 form a complex in vivo that co-localizes in foci associated with arrested replication forks [10].
  • Overexpression of the RAD52 epistasis group of gene products is a convenient way to investigate their in vivo roles in homologous recombination (HR) and DNA repair [11].
  • CONCLUSION: Our findings suggest that genetic polymorphisms of RAD52, ERCC1, and hMLH1 may be associated with breast cancer risk in Korean women [12].
  • In this study, we report three different isoforms of human RAD52 isolated from brain and testis cDNA libraries. cDNAs of these isoforms contain distinct insertions and encode truncated proteins due to translational frame-shifts [13].

Anatomical context of RAD52


Associations of RAD52 with chemical compounds


Physical interactions of RAD52

  • WRN interacts physically and functionally with the recombination mediator protein RAD52 [10].
  • It appears that the RPA32CTD can substitute for RPA70 in binding Rad52 [20].

Co-localisations of RAD52

  • Consistently, immunofluorescence microscopy demonstrated that the hyperphosphorylated RPA was able to co-localize with Rad52 and ATR to form significant nuclear foci in cells [21].

Regulatory relationships of RAD52

  • Therefore, we suggest that excess Rad52p can inhibit the essential RAD51-dependent pathways of HR most likely to be responsible for gene targeting, while at the same time stimulating the RAD51-independent pathway thought to be responsible for extrachromosomal HR [11].

Other interactions of RAD52

  • RAD51, RAD52, and RAD54 encode proteins that are critical to the repair of double-strand DNA breaks by homologous recombination [1].
  • Here we report a novel physical and functional interaction between WRN and the homologous recombination mediator protein RAD52 [10].
  • These findings suggest that RAD54B may play an active role in recombination processes in concert with other members of the RAD52 epistasis group [22].
  • In contrast, relatively fewer genes were down-regulated and these involved IGFBPs, versican, interleukin-1, tumor necrosis factor receptor, CD44, and RAD52 [23].
  • Physical interaction between human RAD52 and RPA is required for homologous recombination in mammalian cells [24].

Analytical, diagnostic and therapeutic context of RAD52


  1. Common nonsense mutations in RAD52. Bell, D.W., Wahrer, D.C., Kang, D.H., MacMahon, M.S., FitzGerald, M.G., Ishioka, C., Isselbacher, K.J., Krainer, M., Haber, D.A. Cancer Res. (1999) [Pubmed]
  2. Precise binding of single-stranded DNA termini by human RAD52 protein. Parsons, C.A., Baumann, P., Van Dyck, E., West, S.C. EMBO J. (2000) [Pubmed]
  3. RAD52 Y415X truncation polymorphism and epithelial ovarian cancer risk in Australian women. Kelemen, L., Spurdle, A.B., Purdie, D.M., Gertig, D., Chenevix-Trench, G. Cancer Lett. (2005) [Pubmed]
  4. Rad52-mediated DNA annealing after Rad51-mediated DNA strand exchange promotes second ssDNA capture. Sugiyama, T., Kantake, N., Wu, Y., Kowalczykowski, S.C. EMBO J. (2006) [Pubmed]
  5. Identification of a human RAD52 pseudogene located on chromosome 2. Johnson, B.L., Campbell, C. Gene (1996) [Pubmed]
  6. AID-dependent generation of resected double-strand DNA breaks and recruitment of Rad52/Rad51 in somatic hypermutation. Zan, H., Wu, X., Komori, A., Holloman, W.K., Casali, P. Immunity (2003) [Pubmed]
  7. In vitro evidence for homologous recombinational repair in resistance to melphalan. Wang, Z.M., Chen, Z.P., Xu, Z.Y., Christodoulopoulos, G., Bello, V., Mohr, G., Aloyz, R., Panasci, L.C. J. Natl. Cancer Inst. (2001) [Pubmed]
  8. Suppression of retroviral infection by the RAD52 DNA repair protein. Lau, A., Kanaar, R., Jackson, S.P., O'Connor, M.J. EMBO J. (2004) [Pubmed]
  9. XRCC3 deficiency results in a defect in recombination and increased endoreduplication in human cells. Yoshihara, T., Ishida, M., Kinomura, A., Katsura, M., Tsuruga, T., Tashiro, S., Asahara, T., Miyagawa, K. EMBO J. (2004) [Pubmed]
  10. WRN interacts physically and functionally with the recombination mediator protein RAD52. Baynton, K., Otterlei, M., Bjørås, M., von Kobbe, C., Bohr, V.A., Seeberg, E. J. Biol. Chem. (2003) [Pubmed]
  11. Differential effects of Rad52p overexpression on gene targeting and extrachromosomal homologous recombination in a human cell line. Yáñez, R.J., Porter, A.C. Nucleic Acids Res. (2002) [Pubmed]
  12. Genetic polymorphisms of selected DNA repair genes, estrogen and progesterone receptor status, and breast cancer risk. Lee, K.M., Choi, J.Y., Kang, C., Kang, C.P., Park, S.K., Cho, H., Cho, D.Y., Yoo, K.Y., Noh, D.Y., Ahn, S.H., Park, C.G., Wei, Q., Kang, D. Clin. Cancer Res. (2005) [Pubmed]
  13. Identification of novel isoforms of human RAD52. Kito, K., Wada, H., Yeh, E.T., Kamitani, T. Biochim. Biophys. Acta (1999) [Pubmed]
  14. Increased expression of human DNA repair genes, XRCC1, XRCC3 and RAD51, in radioresistant human KB carcinoma cell line N10. Yanagisawa, T., Urade, M., Yamamoto, Y., Furuyama, J. Oral Oncol. (1998) [Pubmed]
  15. Structure of the single-strand annealing domain of human RAD52 protein. Singleton, M.R., Wentzell, L.M., Liu, Y., West, S.C., Wigley, D.B. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  16. Overexpression of human RAD51 and RAD52 reduces double-strand break-induced homologous recombination in mammalian cells. Kim, P.M., Allen, C., Wagener, B.M., Shen, Z., Nickoloff, J.A. Nucleic Acids Res. (2001) [Pubmed]
  17. Proteomic changes during the B cell development. Kim, D.R. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. (2005) [Pubmed]
  18. Human RAD52 protein has extreme thermal stability. Ranatunga, W., Jackson, D., Flowers II, R.A., Borgstahl, G.E. Biochemistry (2001) [Pubmed]
  19. Chl1 and Ctf4 are required for damage-induced recombinations. Ogiwara, H., Ui, A., Lai, M.S., Enomoto, T., Seki, M. Biochem. Biophys. Res. Commun. (2007) [Pubmed]
  20. Analysis of the human replication protein A:Rad52 complex: evidence for crosstalk between RPA32, RPA70, Rad52 and DNA. Jackson, D., Dhar, K., Wahl, J.K., Wold, M.S., Borgstahl, G.E. J. Mol. Biol. (2002) [Pubmed]
  21. Preferential localization of hyperphosphorylated replication protein A to double-strand break repair and checkpoint complexes upon DNA damage. Wu, X., Yang, Z., Liu, Y., Zou, Y. Biochem. J. (2005) [Pubmed]
  22. Mutations of a novel human RAD54 homologue, RAD54B, in primary cancer. Hiramoto, T., Nakanishi, T., Sumiyoshi, T., Fukuda, T., Matsuura, S., Tauchi, H., Komatsu, K., Shibasaki, Y., Inui, H., Watatani, M., Yasutomi, M., Sumii, K., Kajiyama, G., Kamada, N., Miyagawa, K., Kamiya, K. Oncogene (1999) [Pubmed]
  23. Growth-associated gene expression profiles by microarray analysis of trophoblast of molar pregnancies and normal villi. Kato, H.D., Terao, Y., Ogawa, M., Matsuda, T., Arima, T., Kato, K., Yong, Z., Wake, N. Int. J. Gynecol. Pathol. (2002) [Pubmed]
  24. Physical interaction between human RAD52 and RPA is required for homologous recombination in mammalian cells. Park, M.S., Ludwig, D.L., Stigger, E., Lee, S.H. J. Biol. Chem. (1996) [Pubmed]
  25. The human Rad52 protein exists as a heptameric ring. Stasiak, A.Z., Larquet, E., Stasiak, A., Müller, S., Engel, A., Van Dyck, E., West, S.C., Egelman, E.H. Curr. Biol. (2000) [Pubmed]
  26. Schizosaccharomyces pombe Rad22A and Rad22B have similar biochemical properties and form multimeric structures. de Vries, F.A., Zonneveld, J.B., de Groot, A.J., Koning, R.I., van Zeeland, A.A., Pastink, A. Mutat. Res. (2007) [Pubmed]
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