Sequence in raw or FASTA format:
RAD50 Rad50p [
Saccharomyces cerevisiae S288c ]
Gene Symbol RAD50
Entrez Gene ID
Full Name Rad50p
General protein information
Subunit of MRX complex with Mre11p and Xrs2p; complex is involved in processing double-strand DNA breaks in vegetative cells, initiation of meiotic DSBs, telomere maintenance, and nonhomologous end joining; forms nuclear foci upon DNA replication stress
Gene Type protein-coding
Saccharomyces cerevisiae S288c ()
WP377 Genes of Meiotic Recombination
5369282 Cell Cycle
5369789 Meiotic recombination
5369396 MRN complex relocalizes to nuclear foci
5369372 DNA Repair
5369394 Double-Strand Break Repair
5369393 Homologous Recombination Repair
5369392 Homologous recombination repair of replication-independent double-strand breaks
5369395 Assembly of the RAD50-MRE11-NBS1 complex at DNA double-strand breaks
5369397 Recruitment of repair and signaling proteins to double-strand breaks
ID Name Evidence
GO:0000706 meiotic DNA double-strand break processing TAS
GO:0000722 telomere maintenance via recombination IMP
GO:0000723 telomere maintenance IMP
GO:0000727 double-strand break repair via break-induced replication TAS
GO:0006281 DNA repair IEA
GO:0006284 base-excision repair IMP
GO:0006303 double-strand break repair via nonhomologous end joining IMP
GO:0006974 cellular response to DNA damage stimulus IEA
GO:0007126 meiotic nuclear division IEA
GO:0007126 meiotic nuclear division IMP
GO:0032078 negative regulation of endodeoxyribonuclease activity IDA
GO:0042138 meiotic DNA double-strand break formation TAS
GO:0097552 mitochondrial double-strand break repair via homologous recombination IMP
Related articles in PubMed Processing of DNA double-stranded breaks and intermediates of recombination and repair by Saccharomyces cerevisiae Mre11 and its stimulation by Rad50, Xrs2, and Sae2 proteins. Ghodke I, et al. J Biol Chem, 2013 Apr 19. PMID 23443654. MRX protects fork integrity at protein-DNA barriers, and its absence causes checkpoint activation dependent on chromatin context. Bentsen IB, et al. Nucleic Acids Res, 2013 Mar 1. PMID 23376930. The generation of oxidative stress-induced rearrangements in Saccharomyces cerevisiae mtDNA is dependent on the Nuc1 (EndoG/ExoG) nuclease and is enhanced by inactivation of the MRX complex. Dzierzbicki P, et al. Mutat Res, 2012 Dec. PMID 23276591. Senataxin associates with replication forks to protect fork integrity across RNA-polymerase-II-transcribed genes. Alzu A, et al. Cell, 2012 Nov 9. PMID 23141540. Multiple pathways regulate minisatellite stability during stationary phase in yeast. Kelly MK, et al. G3 (Bethesda), 2012 Oct. PMID 23050229. See all (161) citations in PubMed See citations in PubMed for homologs of this gene provided by HomoloGene
GeneRIFs: Gene References Into Functions
What's a GeneRIF?
Processing of DNA double-stranded breaks and intermediates of recombination and repair by Saccharomyces cerevisiae Mre11 and its stimulation by Rad50, Xrs2, and Sae2 proteins.
Title: Processing of DNA double-stranded breaks and intermediates of recombination and repair by Saccharomyces cerevisiae Mre11 and its stimulation by Rad50, Xrs2, and Sae2 proteins.
A pivotal role for the MRX (Mre11, Rad50, Xrs2) complex for fork integrity at replication forks.
Title: MRX protects fork integrity at protein-DNA barriers, and its absence causes checkpoint activation dependent on chromatin context.
cohesin loading at replication sites depends on the structural features of Rad50 that are important for bridging sister chromatids, including the CXXC hook domain and the length of the coiled-coil extensions
Title: Cohesin association to replication sites depends on rad50 and promotes fork restart.
deletion of RAD50 may block the major pathway of nonhomologous integration into a non-repetitive chromosomal locus; Rad50 may be involved in facilitating nonhomologous integration of both ends of the integrating DNA into a single chromosomal locus
Title: Effect of rad50 mutation on illegitimate recombination in Saccharomyces cerevisiae.
Study established that Dna2, Sgs1 and RPA constitute a minimal protein complex capable of DNA resection in vitro; in addition it was found that both the Top3 and Rmi1 complex and the Mre11-Rad50-Xrs2 complex have important roles as stimulatory components.
Title: DNA end resection by Dna2-Sgs1-RPA and its stimulation by Top3-Rmi1 and Mre11-Rad50-Xrs2.
a direct role for the Mre11-Rad50-Xrs2 complex in the base excision repair process, which contributes to resistance against base-damaging agents and to the avoidance of mutations
Title: A novel function for the Mre11-Rad50-Xrs2 complex in base excision repair.
The Rad50/Mre11/Xrs2 complex is responsible for rapid processing of most damaged ends into substrates that subsequently undergo recombinational repair.
Title: RAD50 is required for efficient initiation of resection and recombinational repair at random, gamma-induced double-strand break ends.
The Mre11/Rad50/Xrs2 (MRX) complex is essential for joining of incompatible ends by non-homologous end-joining during DNA repair, and the adenosine triphosphate (ATP)-dependent activities of Rad50 are critical for this process.
Title: The Mre11/Rad50/Xrs2 complex and non-homologous end-joining of incompatible ends in S. cerevisiae.
Recombinant Sae2 binds DNA and exhibits endonuclease activity on single-stranded DNA independently of Mre11/Rad50 complexes, but hairpin DNA structures are cleaved cooperatively in the presence of Mre11/Rad50 or Mre11/Rad50/Xrs2.
Title: Sae2 is an endonuclease that processes hairpin DNA cooperatively with the Mre11/Rad50/Xrs2 complex.
Data show that the Saccharomyces cerevisiae MRX complex, or its subunits Mre11/Rad50/Xrs2, prefer G-quadruplex DNA much more than telomeric single-stranded or double-stranded DNA, implicating the possible existence of this DNA structure in vivo.
Title: The characterization of Saccharomyces cerevisiae Mre11/Rad50/Xrs2 complex reveals that Rad50 negatively regulates Mre11 endonucleolytic but not the exonucleolytic activity.
Our customer service representatives are available 24 hours a day, Monday through Friday; please contact us anytime for assistance.