Files in this item
hSSB1 interacts directly with the MRN complex stimulating its recruitment to DNA double-strand breaks and its endo-nuclease activity
Item metadata
dc.contributor.author | Richard, Derek J. | |
dc.contributor.author | Cubeddu, Liza | |
dc.contributor.author | Urquhart, Aaron J. | |
dc.contributor.author | Bain, Amanda | |
dc.contributor.author | Bolderson, Emma | |
dc.contributor.author | Menon, Dinoop | |
dc.contributor.author | White, Malcolm F. | |
dc.contributor.author | Khanna, Kum Kum | |
dc.date.accessioned | 2013-03-27T15:31:12Z | |
dc.date.available | 2013-03-27T15:31:12Z | |
dc.date.issued | 2011-05 | |
dc.identifier | 9375546 | |
dc.identifier | db271bb5-1726-4332-8a07-8d41c5ba32c8 | |
dc.identifier | 000290589500020 | |
dc.identifier | 79956004104 | |
dc.identifier.citation | Richard , D J , Cubeddu , L , Urquhart , A J , Bain , A , Bolderson , E , Menon , D , White , M F & Khanna , K K 2011 , ' hSSB1 interacts directly with the MRN complex stimulating its recruitment to DNA double-strand breaks and its endo-nuclease activity ' , Nucleic Acids Research , vol. 39 , no. 9 , pp. 3643-3651 . https://doi.org/10.1093/nar/gkq1340 | en |
dc.identifier.issn | 0305-1048 | |
dc.identifier.other | ORCID: /0000-0003-1543-9342/work/47136133 | |
dc.identifier.uri | https://hdl.handle.net/10023/3439 | |
dc.description.abstract | hSSB1 is a recently discovered single-stranded DNA binding protein that is essential for efficient repair of DNA double-strand breaks (DSBs) by the homologous recombination pathway. hSSB1 is required for the efficient recruitment of the MRN complex to sites of DSBs and for the efficient initiation of ATM dependent signalling. Here we explore the interplay between hSSB1 and MRN. We demonstrate that hSSB1 binds directly to NBS1, a component of the MRN complex, in a DNA damage independent manner. Consistent with the direct interaction, we observe that hSSB1 greatly stimulates the endo-nuclease activity of the MRN complex, a process that requires the C-terminal tail of hSSB1. Interestingly, analysis of two point mutations in NBS1, associated with Nijmegen breakage syndrome, revealed weaker binding to hSSB1, suggesting a possible disease mechanism. | |
dc.format.extent | 9 | |
dc.format.extent | 4106206 | |
dc.language.iso | eng | |
dc.relation.ispartof | Nucleic Acids Research | en |
dc.subject | Replication protein-a | en |
dc.subject | Binding-protein | en |
dc.subject | Homologous recombination | en |
dc.subject | MRE11-RAD50-NBS1 COMPLEX | en |
dc.subject | Genomic stability | en |
dc.subject | S-phase | en |
dc.subject | ATM | en |
dc.subject | Activation | en |
dc.subject | MRE11 | en |
dc.subject | Checkpoint | en |
dc.subject | QH426 Genetics | en |
dc.subject.lcc | QH426 | en |
dc.title | hSSB1 interacts directly with the MRN complex stimulating its recruitment to DNA double-strand breaks and its endo-nuclease activity | en |
dc.type | Journal article | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.identifier.doi | 10.1093/nar/gkq1340 | |
dc.description.status | Peer reviewed | en |
This item appears in the following Collection(s)
Items in the St Andrews Research Repository are protected by copyright, with all rights reserved, unless otherwise indicated.