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SPO11 protein (Saccharomyces cerevisiae) - STRING interaction network
"SPO11" - Meiosis-specific protein that initiates meiotic recombination by catalyzing the formation of double-strand breaks in DNA via a transesterification reaction in Saccharomyces cerevisiae
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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SPO11Meiosis-specific protein that initiates meiotic recombination by catalyzing the formation of double-strand breaks in DNA via a transesterification reaction; required for homologous chromosome pairing and synaptonemal complex formation; Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. The action of SPO11 is important in setting off a regulatory chain of events encompassing 5’ to 3’ resection. When there are no SPO11-DSBs, resection of a site specific VDE-DSB takes place but it is faster than in wild- [...] (398 aa)    
Predicted Functional Partners:
RAD50
Subunit of MRX complex, with Mre11p and Xrs2p, involved in processing double-strand DNA breaks in vegetative cells, initiation of meiotic DSBs, telomere maintenance, and nonhomologous end joining; Involved in DNA double-strand break repair (DSBR). The rad50/mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific exonuclease activity. Rad50 provides ATP-dependent control of mre11 by unwinding and/or repositioning DNA ends into the mre11 active site (1312 aa)
     
  0.998
MRE11
Subunit of a complex with Rad50p and Xrs2p (MRX complex) that functions in repair of DNA double-strand breaks and in telomere stability, exhibits nuclease activity that appears to be required for MRX function; widely conserved; Involved in DNA double-strand break repair (DSBR). Possesses single-strand endonuclease activity and double-strand- specific 3’-5’ exonuclease activity. Also involved in meiotic DSB processing (692 aa)
     
  0.994
DMC1
Meiosis-specific protein required for repair of double-strand breaks and pairing between homologous chromosomes; homolog of Rad51p and the bacterial RecA protein; Required for meiotic recombination, synaptonemal complex formation and cell cycle progression. Recruited to meiosis recombination hotspots by MEI5 and SAE3 (334 aa)
     
 
  0.993
SAE2
Endonuclease that processes hairpin DNA structures with the MRX complex; involved in meiotic and mitotic double-strand break repair; phosphorylated in response to DNA damage and required for normal resistance to DNA-damaging agents; Endonuclease that cooperates with the MRX complex in processing meiotic and mitotic double-strand breaks by allowing the endonucleolytic removal of SPO11 from the break sites and ensuring both resection and intrachromosomal association of the broken ends. Required for proper recovery from checkpoint-mediated cell cycle arrest after DNA damage. MRX complex a [...] (345 aa)
       
  0.980
REC8
Meiosis-specific component of sister chromatid cohesion complex; maintains cohesion between sister chromatids during meiosis I; maintains cohesion between centromeres of sister chromatids until meiosis II; homolog of S. pombe Rec8p; Replaces the SCC1 mitosis-specific cohesin to ensure sister chromatid cohesion during meiosis. Is cleaved by ESP1 shortly before the first meiotic division, and dissociates from chromatin, allowing sister chromatids to segregate. Is protected from cleavage by SPO13 (680 aa)
     
 
  0.973
MEC1
Genome integrity checkpoint protein and PI kinase superfamily member; signal transducer required for cell cycle arrest and transcriptional responses prompted by damaged or unreplicated DNA; monitors and participates in meiotic recombination; Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Recruited in complex with protein LCD1 by the single-strand-binding protein comp [...] (2368 aa)
       
 
  0.969
MSH4
Protein involved in meiotic recombination, required for normal levels of crossing over, colocalizes with Zip2p to discrete foci on meiotic chromosomes, has homology to bacterial MutS protein; Involved in meiotic recombination. Facilitate crossovers between homologs during meiosis (878 aa)
     
 
  0.965
SKI8
Ski complex component and WD-repeat protein, mediates 3’-5’ RNA degradation by the cytoplasmic exosome; also required for meiotic double-strand break recombination; null mutants have superkiller phenotype; Involved in double-strand break (DSB) formation during meiotic recombination through stabilization of SPO11 association with meiotic chromosome and helping SPO11 to recruit other DSB proteins like REC102 and REC104 to meiotic chromosomes. Also component of the SKI complex involved in 3’-mRNA degradation pathway. Represses dsRNA virus propagation by specifically blocking translation o [...] (397 aa)
       
 
  0.961
MUS81
Subunit of the structure-specific Mms4p-Mus81p endonuclease that cleaves branched DNA; involved in DNA repair, replication fork stability, and joint molecule formation/resolution during meiotic recombination; helix-hairpin-helix protein; Interacts with MMS4 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5’-end at the branch nick. Typical substrates include 3’- flap structures, D-loops, replication forks with regressed leading strands and nicked Holliday junctions. Cleavage probably occurs approximately half a helical turn upst [...] (632 aa)
     
 
  0.959
RAD51
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; Required both for recombination and for the repair of DNA damage caused by X-rays. Its function may be modulated by interaction with other repair proteins. RAD52 interacts directly with RAD51, via its C-terminus. Forms a nucleoprotein filament with DNA as an early intermediate in recombination (400 aa)
     
 
  0.958
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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