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dc.contributor.authorGrundy, GJ
dc.contributor.authorRulten, SL
dc.contributor.authorArribas-Bosacoma, R
dc.contributor.authorDavidson, K
dc.contributor.authorKozik, Z
dc.contributor.authorOliver, AW
dc.contributor.authorPearl, LH
dc.contributor.authorCaldecott, KW
dc.date.accessioned2020-06-22T15:47:34Z
dc.date.issued2016-04-11
dc.identifier.citationNature communications, 2016, 7 pp. 11242 - ?
dc.identifier.issn2041-1723
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/3766
dc.identifier.eissn2041-1723
dc.identifier.doi10.1038/ncomms11242
dc.description.abstractThe Ku-binding motif (KBM) is a short peptide module first identified in APLF that we now show is also present in Werner syndrome protein (WRN) and in Modulator of retrovirus infection homologue (MRI). We also identify a related but functionally distinct motif in XLF, WRN, MRI and PAXX, which we denote the XLF-like motif. We show that WRN possesses two KBMs; one at the N terminus next to the exonuclease domain and one at the C terminus next to an XLF-like motif. We reveal that the WRN C-terminal KBM and XLF-like motif function cooperatively to bind Ku complexes and that the N-terminal KBM mediates Ku-dependent stimulation of WRN exonuclease activity. We also show that WRN accelerates DSB repair by a mechanism requiring both KBMs, demonstrating the importance of WRN interaction with Ku. These data define a conserved family of KBMs that function as molecular tethers to recruit and/or stimulate enzymes during NHEJ.
dc.formatElectronic
dc.format.extent11242 - ?
dc.languageeng
dc.language.isoeng
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.subjectHumans
dc.subjectDNA Damage
dc.subjectExodeoxyribonucleases
dc.subjectDNA-Binding Proteins
dc.subjectAntigens, Nuclear
dc.subjectAmino Acid Sequence
dc.subjectAmino Acid Motifs
dc.subjectConserved Sequence
dc.subjectProtein Structure, Tertiary
dc.subjectProtein Binding
dc.subjectModels, Biological
dc.subjectMolecular Sequence Data
dc.subjectRecQ Helicases
dc.subjectDNA Breaks, Double-Stranded
dc.subjectDNA End-Joining Repair
dc.subjectKu Autoantigen
dc.subjectWerner Syndrome Helicase
dc.titleThe Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins.
dc.typeJournal Article
dcterms.dateAccepted2016-03-04
rioxxterms.versionofrecord10.1038/ncomms11242
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0
rioxxterms.licenseref.startdate2016-04-11
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfNature communications
pubs.notesNot known
pubs.organisational-group/ICR
pubs.organisational-group/ICR
pubs.publication-statusPublished
pubs.volume7en_US
pubs.embargo.termsNot known
dc.contributor.icrauthorPearl, Laurenceen


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