Alternative titles; symbols
HGNC Approved Gene Symbol: RAD52
Cytogenetic location: 12p13.33 Genomic coordinates (GRCh38): 12:911,736-991,122 (from NCBI)
Ionizing radiation causes different types of DNA damage. Misrepair or nonrepair of this damage may cause cell death, mutation, and neoplastic transformation. Distinctive pathways of DNA repair respond to different DNA damage. In Saccharomyces cerevisiae, 3 epistasis groups of DNA damage-repair genes have been identified. The RAD52 epistasis group, which is mainly responsible for DNA double-strand break repair, contains 8 genes: RAD50 through RAD57. One of these, RAD51 (179617), has been cloned and found to have homology in yeast, chicken, mouse, and human to the bacterial Rec-A (RECA) protein, which is required for homologous recombination. See also RAD54L (603615). The RAD52 gene of Saccharomyces cerevisiae is involved in DNA double-strand break repair and mitotic/meiotic recombination. The N-terminal amino acid sequence is highly conserved across species.
Using the technology of mixed oligonucleotide primed amplification of cDNA (MOPAC), Shen et al. (1995) amplified and sequenced 2 mouse RAD52 homologous cDNA fragments. Subsequently, they cloned cDNA of the human and mouse homologs of the yeast RAD52 gene by screening cDNA libraries using the identified mouse cDNA fragments.
The human RAD52 protein forms a heptameric ring that catalyzes homologous pairing. The N-terminal half of RAD52 is the catalytic domain for homologous pairing, and the ring formed by the domain fragment was reported to be approximately decameric. Splicing variants of RAD52 and a yeast homolog, Rad59, are composed mostly of this domain. Kagawa et al. (2002) determined the crystal structure of the homologous-pairing domain of human RAD52 and found that the domain forms an undecameric ring. Each monomer has a beta-beta-beta-alpha fold, which consists of highly conserved amino acid residues among RAD52 homologs. A mutational analysis revealed that the amino acid residues located between the beta-beta-beta-alpha fold and the characteristic hairpin loop are essential for single-stranded DNA and double-stranded DNA binding.
By DNA analysis of somatic cell hybrids and by fluorescence in situ hybridization, Shen et al. (1995) assigned the human RAD52 gene to 12p13-p12.2.
Kagawa, W., Kurumizaka, H., Ishitani, R., Fukai, S., Nureki, O., Shibata, T., Yokoyama, S. Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form. Molec. Cell 10: 359-371, 2002. [PubMed: 12191481] [Full Text: https://doi.org/10.1016/s1097-2765(02)00587-7]
Shen, Z., Denison, K., Lobb, R., Gatewood, J. M., Chen, D. J. The human and mouse homologs of the yeast RAD52 gene: cDNA cloning, sequence analysis, assignment to human chromosome 12p12.2-p13, and mRNA expression in mouse tissues. Genomics 25: 199-206, 1995. [PubMed: 7774919] [Full Text: https://doi.org/10.1016/0888-7543(95)80126-7]