RAD52/YML032C Summary Help

Standard Name RAD52
Systematic Name YML032C
Feature Type ORF, Verified
Description Protein that stimulates strand exchange; stimulates strand exchange by facilitating Rad51p binding to single-stranded DNA; anneals complementary single-stranded DNA; involved in the repair of double-strand breaks in DNA during vegetative growth and meiosis and UV induced sister chromatid recombination (1, 2, 3, 4, 5 and see Summary Paragraph)
Name Description RADiation sensitive
Chromosomal Location
ChrXIII:213930 to 212515 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Genetic position: -18 cM
Gene Ontology Annotations All RAD52 GO evidence and references
  View Computational GO annotations for RAD52
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 7 genes
Resources
Classical genetics
null
reduction of function
Large-scale survey
null
overexpression
unspecified
Resources
1001 total interaction(s) for 412 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 31
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 27
  • Biochemical Activity: 5
  • Co-localization: 7
  • Reconstituted Complex: 17
  • Two-hybrid: 23

Genetic Interactions
  • Dosage Growth Defect: 1
  • Dosage Lethality: 2
  • Dosage Rescue: 13
  • Negative Genetic: 198
  • Phenotypic Enhancement: 128
  • Phenotypic Suppression: 60
  • Positive Genetic: 53
  • Synthetic Growth Defect: 268
  • Synthetic Lethality: 107
  • Synthetic Rescue: 59

Resources
Expression Summary
histogram
Resources
Length (a.a.) 471
Molecular Weight (Da) 52,403
Isoelectric Point (pI) 8.56
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXIII:213930 to 212515 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Genetic position: -18 cM
Last Update Coordinates: 2003-01-07 | Sequence: 2003-01-07
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1416 213930..212515 2003-01-07 2003-01-07
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | Entrez Gene | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000004494
SUMMARY PARAGRAPH for RAD52

Identified in a genetic screen for mutants that are sensitive to ionizing radiation (6), RAD52 is a member of the RAD52 epistasis group. Other members of this group include RAD50, RAD51, RAD54, RAD55, RAD57, RAD59, MRE11, and XRS2. All members of the RAD52 epistasis group are involved in the repair of double-stranded breaks (DSBs) in DNA. Mutants are defective in the repair of DNA damage cause by ionizing radiation and MMS and in the maintenance of telomere length, in mitotic and meiotic recombination, and in mating-type switching because DSB intermediates are involved in these processes (reviewed in 7, 4). Of all the members of the RAD52 epistasis group, the absence of RAD52 confers the most severe defects because it is involved in multiple pathways of repairing DSBs. RAD52 plays a role in the RAD51-dependent double-strand break repair (DSBR) pathway, known as synthesis-dependent strand annealing (SDSA) as well as in RAD51-independent DSBR pathways, known as break-induced replication (BIR) and single-strand annealing (SSA) (review in 7).

Biochemical studies of Rad52p give insight into its role in multiple DSBR pathways. Rad52p stimulates the Rad51p recombinase activty (8, 2, 9). Rad52p interacts with Rad51p and Replication Protein A (RPA), which is comprised of Rfa1p, Rfa2p, and Rfa3p (10, 11). These interactions may facilitate the formation of Rad51p:single-stranded DNA nucleoprotein filaments in the presence of RPA (12, 13). In addition, Rad52p anneals complementary strands of ssDNA (3, 14). Rad52p also interacts with Rad59p, an interaction that may be important in its Rad51-independent DSB repair pathways (15).

Although RAD52 is expressed throughout the cell cycle, it is induced during meiosis and in response to DNA damaging agents (16, 17). A Rad52p-GFP fusion forms nuclear foci in the absence and presence of DNA damaging agents (18). Electron microscopic studies of purified yeast Rad52p shows that it forms a ring structure but it is not clear how Rad52p binds DNA (14).

Orthologs of RAD52 have been identified in many organisms, including chicken, S. pombe, mice, and humans (19, 20, 21). In contrast to the situation in yeast, the absence of RAD52 in higher eukaryotes does not result in a severe phenotype (22, 23) because there are additional functionally redundant proteins (24, reviewed in 25).

Last updated: 2003-01-06 Contact SGD

References cited on this page View Complete Literature Guide for RAD52
1) Adzuma K, et al.  (1984) Primary structure of the RAD52 gene in Saccharomyces cerevisiae. Mol Cell Biol 4(12):2735-44
2) Shinohara A and Ogawa T  (1998) Stimulation by Rad52 of yeast Rad51-mediated recombination. Nature 391(6665):404-7
3) Mortensen UH, et al.  (1996) DNA strand annealing is promoted by the yeast Rad52 protein. Proc Natl Acad Sci U S A 93(20):10729-34
4) Symington LS  (2002) Role of RAD52 epistasis group genes in homologous recombination and double-strand break repair. Microbiol Mol Biol Rev 66(4):630-70, table of contents
5) Prakash L and Taillon-Miller P  (1981) Effects of the rad52 gene on sister chromatid recombination in Saccharomyces cerevisiae. Curr Genet 3(3):247-50
6) Game JC and Mortimer RK  (1974) A genetic study of x-ray sensitive mutants in yeast. Mutat Res 24(3):281-92
7) Paques F and Haber JE  (1999) Multiple pathways of recombination induced by double-strand breaks in Saccharomyces cerevisiae. Microbiol Mol Biol Rev 63(2):349-404
8) Sung P  (1997) Function of yeast Rad52 protein as a mediator between replication protein A and the Rad51 recombinase. J Biol Chem 272(45):28194-7
9) New JH, et al.  (1998) Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein A. Nature 391(6665):407-10
10) Shinohara A, et al.  (1992) Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein. Cell 69(3):457-70
11) Hays SL, et al.  (1998) Studies of the interaction between Rad52 protein and the yeast single-stranded DNA binding protein RPA. Mol Cell Biol 18(7):4400-6
12) Gasior SL, et al.  (2001) Assembly of RecA-like recombinases: distinct roles for mediator proteins in mitosis and meiosis. Proc Natl Acad Sci U S A 98(15):8411-8
13) Sugiyama T and Kowalczykowski SC  (2002) Rad52 protein associates with replication protein A (RPA)-single-stranded DNA to accelerate Rad51-mediated displacement of RPA and presynaptic complex formation. J Biol Chem 277(35):31663-72
14) Shinohara A, et al.  (1998) Rad52 forms ring structures and co-operates with RPA in single-strand DNA annealing. Genes Cells 3(3):145-56
15) Davis AP and Symington LS  (2001) The yeast recombinational repair protein Rad59 interacts with Rad52 and stimulates single-strand annealing. Genetics 159(2):515-25
16) Cole GM, et al.  (1987) Regulation of RAD54- and RAD52-lacZ gene fusions in Saccharomyces cerevisiae in response to DNA damage. Mol Cell Biol 7(3):1078-84
17) Cole GM, et al.  (1989) Two DNA repair and recombination genes in Saccharomyces cerevisiae, RAD52 and RAD54, are induced during meiosis. Mol Cell Biol 9(7):3101-4
18) Lisby M, et al.  (2001) Rad52 forms DNA repair and recombination centers during S phase. Proc Natl Acad Sci U S A 98(15):8276-82
19) Bezzubova OY, et al.  (1993) Identification of a chicken RAD52 homologue suggests conservation of the RAD52 recombination pathway throughout the evolution of higher eukaryotes. Nucleic Acids Res 21(25):5945-9
20) Ostermann K, et al.  (1993) The fission yeast rad22 gene, having a function in mating-type switching and repair of DNA damages, encodes a protein homolog to Rad52 of Saccharomyces cerevisiae. Nucleic Acids Res 21(25):5940-4
21) Muris DF, et al.  (1994) Cloning of human and mouse genes homologous to RAD52, a yeast gene involved in DNA repair and recombination. Mutat Res 315(3):295-305
22) Rijkers T, et al.  (1998) Targeted inactivation of mouse RAD52 reduces homologous recombination but not resistance to ionizing radiation. Mol Cell Biol 18(11):6423-9
23) Yamaguchi-Iwai Y, et al.  (1998) Homologous recombination, but not DNA repair, is reduced in vertebrate cells deficient in RAD52. Mol Cell Biol 18(11):6430-5
24) Fujimori A, et al.  (2001) Rad52 partially substitutes for the Rad51 paralog XRCC3 in maintaining chromosomal integrity in vertebrate cells. EMBO J 20(19):5513-20
25) Sonoda E, et al.  (2001) Homologous DNA recombination in vertebrate cells. Proc Natl Acad Sci U S A 98(15):8388-94