RAD51/YER095W Summary Help

Standard Name RAD51
Systematic Name YER095W
Alias MUT5
Feature Type ORF, Verified
Description Strand exchange protein; forms a helical filament with DNA that searches for homology; involved in the recombinational repair of double-strand breaks in DNA during vegetative growth and meiosis; homolog of Dmc1p and bacterial RecA protein (1, 2, 3 and see Summary Paragraph)
Name Description RADiation sensitive
Chromosomal Location
ChrV:349980 to 351182 | ORF Map | GBrowse
Gbrowse
Genetic position: 78 cM
Gene Ontology Annotations All RAD51 GO evidence and references
  View Computational GO annotations for RAD51
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 9 genes
Resources
Classical genetics
null
reduction of function
Large-scale survey
null
Resources
858 total interaction(s) for 390 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 44
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 15
  • Biochemical Activity: 1
  • Co-crystal Structure: 1
  • Co-fractionation: 1
  • Co-localization: 2
  • PCA: 1
  • Reconstituted Complex: 32
  • Two-hybrid: 52

Genetic Interactions
  • Dosage Growth Defect: 4
  • Dosage Lethality: 2
  • Dosage Rescue: 13
  • Negative Genetic: 150
  • Phenotypic Enhancement: 60
  • Phenotypic Suppression: 57
  • Positive Genetic: 54
  • Synthetic Growth Defect: 174
  • Synthetic Lethality: 128
  • Synthetic Rescue: 66

Resources
Expression Summary
histogram
Resources
Length (a.a.) 400
Molecular Weight (Da) 42,963
Isoelectric Point (pI) 4.64
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrV:349980 to 351182 | ORF Map | GBrowse
SGD ORF map
Genetic position: 78 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1203 349980..351182 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000897
SUMMARY PARAGRAPH for RAD51

Identified in a genetic screen for mutants that are sensitive to ionizing radiation (4), RAD51 is a member of the RAD52 epistasis group. Other members of this group include RAD50, RAD52, 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 caused by ionizing radiation and MMS, 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 5, 3).

A rad51 deletion mutation is not lethal in S. cerevisiae because DSBs can be repaired by multiple pathways. RAD51 is only involved in DSB repair via synthesis-dependent strand annealing (SDSA) and is not involved in DSB repair via break-induced replication (BIR) or single-strand annealing (SSA) (reviewed in 5).

The function of Rad51p was predicted by its structural homology to the bacterial DNA repair protein RecA and the T4 phage protein UvsX (2, 6, 7, reviewed in 8). Rad51p is a recombinase ; it binds DNA (2) and catalyzes the identification and exchange of homologous sequences between a single-strand DNA (ssDNA) molecule and a double-stranded DNA (dsDNA) molecule (1). Rad51p interacts with itself and other members of the RAD52 epistasis group: Rad52p, the Rad55p-Rad57p heterodimer, Rad54p, and Rdh54p/Tid1p (2, 9, 10, 11). These interacting proteins stimulate the assembly of Rad51p onto ssDNA and its recombinase activity (12, 13, 14, 15, 16, 17).

The role of RAD51 in meiosis is complicated by the presence of the meiosis-specific RecA homolog DMC1 (2, 18, 19). Coordination of RAD51 with DMC1 and other members of the RAD52 epistasis group is required to convert DSBs into Holliday junctions (a recombination intermediate) and for full levels of recombinant products (20, 18, 21, 22).

Although RAD51 is expressed throughout the cell cycle, it is induced during meiosis and in response to DNA damaging agents (2, 23). Rad51p forms discrete foci on chromosomes that can be detected cytologically during mitosis and meiosis (review in 24).

Orthologs of RAD51 have been identified in many organisms, including humans, mice, chicken, and X. laevis (25, 26, 27, 28). In contrast to the situation in yeast, the absence of rad51 in higher eukaryotes results in embryonic lethality or cell death (29, 30, 31).

Last updated: 2001-01-03 Contact SGD

References cited on this page View Complete Literature Guide for RAD51
1) Sung P  (1994) Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein. Science 265(5176):1241-3
2) 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
3) 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
4) Game JC and Mortimer RK  (1974) A genetic study of x-ray sensitive mutants in yeast. Mutat Res 24(3):281-92
5) 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
6) Aboussekhra A, et al.  (1992) Semidominant suppressors of Srs2 helicase mutations of Saccharomyces cerevisiae map in the RAD51 gene, whose sequence predicts a protein with similarities to procaryotic RecA proteins. Mol Cell Biol 12(7):3224-34
7) Ogawa T, et al.  (1993) Similarity of the yeast RAD51 filament to the bacterial RecA filament. Science 259(5103):1896-9
8) Bianco PR, et al.  (1998) DNA strand exchange proteins: a biochemical and physical comparison. Front Biosci 3():D570-603
9) Hays SL, et al.  (1995) Complex formation in yeast double-strand break repair: participation of Rad51, Rad52, Rad55, and Rad57 proteins. Proc Natl Acad Sci U S A 92(15):6925-9
10) Jiang H, et al.  (1996) Direct association between the yeast Rad51 and Rad54 recombination proteins. J Biol Chem 271(52):33181-6
11) Dresser ME, et al.  (1997) DMC1 functions in a Saccharomyces cerevisiae meiotic pathway that is largely independent of the RAD51 pathway. Genetics 147(2):533-44
12) 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
13) Sung P  (1997) Yeast Rad55 and Rad57 proteins form a heterodimer that functions with replication protein A to promote DNA strand exchange by Rad51 recombinase. Genes Dev 11(9):1111-21
14) Shinohara A and Ogawa T  (1998) Stimulation by Rad52 of yeast Rad51-mediated recombination. Nature 391(6665):404-7
15) New JH, et al.  (1998) Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein A. Nature 391(6665):407-10
16) Petukhova G, et al.  (1998) Catalysis of homologous DNA pairing by yeast Rad51 and Rad54 proteins. Nature 393(6680):91-4
17) Petukhova G, et al.  (2000) Promotion of Rad51-dependent D-loop formation by yeast recombination factor Rdh54/Tid1. Genes Dev 14(17):2206-15
18) Shinohara A, et al.  (1997) Saccharomyces cerevisiae recA homologues RAD51 and DMC1 have both distinct and overlapping roles in meiotic recombination. Genes Cells 2(10):615-29
19) Bishop DK, et al.  (1992) DMC1: a meiosis-specific yeast homolog of E. coli recA required for recombination, synaptonemal complex formation, and cell cycle progression. Cell 69(3):439-56
20) Bishop DK  (1994) RecA homologs Dmc1 and Rad51 interact to form multiple nuclear complexes prior to meiotic chromosome synapsis. Cell 79(6):1081-92
21) Shinohara M, et al.  (2000) Tid1/Rdh54 promotes colocalization of rad51 and dmc1 during meiotic recombination. Proc Natl Acad Sci U S A 97(20):10814-9
22) Schwacha A and Kleckner N  (1997) Interhomolog bias during meiotic recombination: meiotic functions promote a highly differentiated interhomolog-only pathway. Cell 90(6):1123-35
23) Basile G, et al.  (1992) Nucleotide sequence and transcriptional regulation of the yeast recombinational repair gene RAD51. Mol Cell Biol 12(7):3235-46
24) 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
25) Shinohara A, et al.  (1993) Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA. Nat Genet 4(3):239-43
26) Bezzubova O, et al.  (1993) A chicken RAD51 homologue is expressed at high levels in lymphoid and reproductive organs. Nucleic Acids Res 21(7):1577-80
27) Morita T, et al.  (1993) A mouse homolog of the Escherichia coli recA and Saccharomyces cerevisiae RAD51 genes. Proc Natl Acad Sci U S A 90(14):6577-80
28) Maeshima K, et al.  (1995) RAD51 homologues in Xenopus laevis: two distinct genes are highly expressed in ovary and testis. Gene 160(2):195-200
29) Lim DS and Hasty P  (1996) A mutation in mouse rad51 results in an early embryonic lethal that is suppressed by a mutation in p53. Mol Cell Biol 16(12):7133-43
30) Tsuzuki T, et al.  (1996) Targeted disruption of the Rad51 gene leads to lethality in embryonic mice. Proc Natl Acad Sci U S A 93(13):6236-40
31) Sonoda E, et al.  (1998) Rad51-deficient vertebrate cells accumulate chromosomal breaks prior to cell death. EMBO J 17(2):598-608