RAD57/YDR004W Summary Help

Standard Name RAD57
Systematic Name YDR004W
Feature Type ORF, Verified
Description Protein that stimulates strand exchange; stimulates strand exchange by stabilizing the binding of Rad51p to single-stranded DNA; involved in the recombinational repair of double-strand breaks in DNA during vegetative growth and meiosis; forms heterodimer with Rad55p (1, 2 and see Summary Paragraph)
Name Description RADiation sensitive
Chromosomal Location
ChrIV:455201 to 456583 | ORF Map | GBrowse
Genetic position: 2 cM
Gene Ontology Annotations All RAD57 GO evidence and references
  View Computational GO annotations for RAD57
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 4 genes
Classical genetics
reduction of function
Large-scale survey
275 total interaction(s) for 138 unique genes/features.
Physical Interactions
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 3
  • Reconstituted Complex: 4
  • Two-hybrid: 11

Genetic Interactions
  • Dosage Lethality: 1
  • Dosage Rescue: 2
  • Negative Genetic: 89
  • Phenotypic Enhancement: 6
  • Phenotypic Suppression: 11
  • Positive Genetic: 11
  • Synthetic Growth Defect: 94
  • Synthetic Lethality: 23
  • Synthetic Rescue: 19

Expression Summary
Length (a.a.) 460
Molecular Weight (Da) 52,247
Isoelectric Point (pI) 6.61
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIV:455201 to 456583 | ORF Map | GBrowse
Genetic position: 2 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1383 455201..456583 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000002411

Identified in a genetic screen for mutants that are sensitive to ionizing radiation, RAD57 is a member of the RAD52 epistasis group (3). Other members of this group include RAD50, RAD51, RAD52, RAD54, RAD55, 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 4, 5, 2).

Rad57p functions as a heterodimer with Rad55p (6, 7, 8) to promote the formation of the Rad51p:single-stranded DNA (ssDNA) nucleoprotein filament at the site of a DSB by displacing Replication Protein A (RPA) from ssDNA (8, 9). Formation of the Rad51p:ssDNA filament is required for homology searching and strand exchange during DSB repair via homologous recombination. A Rad51p mutant with a higher ssDNA binding affinity bypasses the need for the Rad55p-Rad57p heterodimer (1). Deletion of RAD51 or overexpression of Rad51p suppresses the cold sensitivity phenotype of a rad55 rad57 double mutant (10, 7). Rad52p also helps assemble Rad51p onto ssDNA (11, 12, 13) but both Rad52p and the Rad55p-Rad57p heterodimer are required for efficient assembly of Rad51p at sites of DSBs during mating-type switching, meiosis, and mitosis (14, 15, 16).

The Rad55p-Rad57p heterodimer is regulated by DNA damage checkpoints (17). Rad55p is phosphorylated by the checkpoint kinase Rad53p in response to DNA damaging agents such as methyl-methane sulfonate (MMS), gamma ray radiation, and UV radiation, as well as collapsed replication forks (17, 18).

Rad55p and Rad57p are paralogs of S. cerevisiae Rad51p (19). RAD51 paralogs in other organisms include Rhp55 and Rhp57 in S. pombe (20, 21), AtXRCC3 and AtRAD51C in A. thaliana (22), and XRCC2, XRCC3, Rad51B, Rad51C, and Rad51D in humans and other vertebrates (reviewed in 23).

Last updated: 2006-11-14 Contact SGD

References cited on this page View Complete Literature Guide for RAD57
1) Fortin GS and Symington LS  (2002) Mutations in yeast Rad51 that partially bypass the requirement for Rad55 and Rad57 in DNA repair by increasing the stability of Rad51-DNA complexes. EMBO J 21(12):3160-70
2) 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
3) Game JC and Mortimer RK  (1974) A genetic study of x-ray sensitive mutants in yeast. Mutat Res 24(3):281-92
4) Krogh BO and Symington LS  (2004) Recombination proteins in yeast. Annu Rev Genet 38():233-71
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) 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
7) Johnson RD and Symington LS  (1995) Functional differences and interactions among the putative RecA homologs Rad51, Rad55, and Rad57. Mol Cell Biol 15(9):4843-50
8) 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
9) Gasior SL, et al.  (1998) Rad52 associates with RPA and functions with rad55 and rad57 to assemble meiotic recombination complexes. Genes Dev 12(14):2208-21
10) Rattray AJ and Symington LS  (1995) Multiple pathways for homologous recombination in Saccharomyces cerevisiae. Genetics 139(1):45-56
11) Song B and Sung P  (2000) Functional interactions among yeast Rad51 recombinase, Rad52 mediator, and replication protein A in DNA strand exchange. J Biol Chem 275(21):15895-904
12) New JH, et al.  (1998) Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein A. Nature 391(6665):407-10
13) Shinohara A and Ogawa T  (1998) Stimulation by Rad52 of yeast Rad51-mediated recombination. Nature 391(6665):404-7
14) Sugawara N, et al.  (2003) In vivo roles of Rad52, Rad54, and Rad55 proteins in Rad51-mediated recombination. Mol Cell 12(1):209-19
15) 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
16) Miyazaki T, et al.  (2004) In vivo assembly and disassembly of Rad51 and Rad52 complexes during double-strand break repair. EMBO J 23(4):939-49
17) Bashkirov VI, et al.  (2000) DNA repair protein Rad55 is a terminal substrate of the DNA damage checkpoints. Mol Cell Biol 20(12):4393-404
18) Herzberg K, et al.  (2006) Phosphorylation of Rad55 on serines 2, 8, and 14 is required for efficient homologous recombination in the recovery of stalled replication forks. Mol Cell Biol 26(22):8396-409
19) Lovett ST  (1994) Sequence of the RAD55 gene of Saccharomyces cerevisiae: similarity of RAD55 to prokaryotic RecA and other RecA-like proteins. Gene 142(1):103-6
20) Khasanov FK, et al.  (1999) A new recombinational DNA repair gene from Schizosaccharomyces pombe with homology to Escherichia coli RecA. Genetics 152(4):1557-72
21) Tsutsui Y, et al.  (2000) A recombination repair gene of Schizosaccharomyces pombe, rhp57, is a functional homolog of the Saccharomyces cerevisiae RAD57 gene and is phylogenetically related to the human XRCC3 gene. Genetics 154(4):1451-61
22) Osakabe K, et al.  (2002) Molecular cloning and characterization of RAD51-like genes from Arabidopsis thaliana. Plant Mol Biol 50(1):71-81
23) Sung P, et al.  (2003) Rad51 recombinase and recombination mediators. J Biol Chem 278(44):42729-32