dc.contributor.author | Grundy, GJ | |
dc.contributor.author | Rulten, SL | |
dc.contributor.author | Arribas-Bosacoma, R | |
dc.contributor.author | Davidson, K | |
dc.contributor.author | Kozik, Z | |
dc.contributor.author | Oliver, AW | |
dc.contributor.author | Pearl, LH | |
dc.contributor.author | Caldecott, KW | |
dc.date.accessioned | 2020-06-22T15:47:34Z | |
dc.date.issued | 2016-04-11 | |
dc.identifier.citation | Nature communications, 2016, 7 pp. 11242 - ? | |
dc.identifier.issn | 2041-1723 | |
dc.identifier.uri | https://repository.icr.ac.uk/handle/internal/3766 | |
dc.identifier.eissn | 2041-1723 | |
dc.identifier.doi | 10.1038/ncomms11242 | |
dc.description.abstract | The 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.format | Electronic | |
dc.format.extent | 11242 - ? | |
dc.language | eng | |
dc.language.iso | eng | |
dc.publisher | NATURE PUBLISHING GROUP | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0 | |
dc.subject | Humans | |
dc.subject | DNA Damage | |
dc.subject | Exodeoxyribonucleases | |
dc.subject | DNA-Binding Proteins | |
dc.subject | Antigens, Nuclear | |
dc.subject | Amino Acid Sequence | |
dc.subject | Amino Acid Motifs | |
dc.subject | Conserved Sequence | |
dc.subject | Protein Structure, Tertiary | |
dc.subject | Protein Binding | |
dc.subject | Models, Biological | |
dc.subject | Molecular Sequence Data | |
dc.subject | RecQ Helicases | |
dc.subject | DNA Breaks, Double-Stranded | |
dc.subject | DNA End-Joining Repair | |
dc.subject | Ku Autoantigen | |
dc.subject | Werner Syndrome Helicase | |
dc.title | The Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins. | |
dc.type | Journal Article | |
dcterms.dateAccepted | 2016-03-04 | |
rioxxterms.versionofrecord | 10.1038/ncomms11242 | |
rioxxterms.licenseref.uri | https://creativecommons.org/licenses/by/4.0 | |
rioxxterms.licenseref.startdate | 2016-04-11 | |
rioxxterms.type | Journal Article/Review | |
dc.relation.isPartOf | Nature communications | |
pubs.notes | Not known | |
pubs.organisational-group | /ICR | |
pubs.organisational-group | /ICR | |
pubs.publication-status | Published | |
pubs.volume | 7 | |
pubs.embargo.terms | Not known | |
dc.contributor.icrauthor | Pearl, Laurence | |