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Details on Person The MRN complex (MRE11:RAD50:NBS1:CtIP) exonucleolytically h...
| Class:Id | Summation:9023940 |
|---|---|
| _displayName | The MRN complex (MRE11:RAD50:NBS1:CtIP) exonucleolytically h... |
| _timestamp | 2017-09-29 09:32:39 |
| created | [InstanceEdit:9023944] May, Bruce, 2017-09-29 |
| text | The MRN complex (MRE11:RAD50:NBS1:CtIP) exonucleolytically hydrolyzes a single strand of DNA in a 3' to 5' direction starting at a single strand break made by the MRN complex 3' to SPO11. SPO11 forms a dimer and each subunit cleaves a single strand of DNA, thus creating a double-strand break. After cleaving DNA, a SPO11 subunit remains covalently attached to each 5' end via a tyrosine residue. SPO11 is removed from the DNA by cleavage and exonucleolytic digestion of single strands 3' to the attached SPO11. The overall products are a resected 5' end (protruding 3' overhang) and a covalent complex of SPO11 with an oligonucleotide. Two size classes of oligonucleotide are observed: 12 to 26 nucleotides and 28 to 34 nucleotides. The enzyme responsible for excision of SPO11:oligonucleotide in mammals is inferred to be MRE11 in the MRE11:RAD50:NBS1:CtIP complex based on conservation of the reaction mechanism across yeast, plants, and animals (Sartori et al. 2007). In fission and budding yeast the Mre11:Rad50:Xrs2/Nbs1 (MRN/MRX) complex is required for removal of SPO11. In human somatic cells the MRN complex together with CtIP resects double-strand breaks but the role of the MRN complex in mammalian meiosis, though essential, is unclear (Sartori et al. 2007). After excision of SPO11:oligonucleotide the recessed 5' end is further resected by unknown exonucleases. |
| (summation) | [BlackBoxEvent:9023943] MRN:CtIP exonucleolytically hydrolyzes DNA 3' to SPO11 and SPO11:double-strand break dissociates to SPO11:oligonucleotide and resected 5' end [Homo sapiens] |
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