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dc.contributor.authorKeka, Islam Shamimaja
dc.contributor.authorMohiuddinja
dc.contributor.authorMaede, Yukoja
dc.contributor.authorRahman, Md Maminurja
dc.contributor.authorSakuma, Tetsushija
dc.contributor.authorHonma, Masamitsuja
dc.contributor.authorYamamoto, Takashija
dc.contributor.authorTakeda, Shunichija
dc.contributor.authorSasanuma, Hiroyukija
dc.contributor.alternative本間, 正充ja
dc.contributor.alternative山本, 卓ja
dc.contributor.alternative武田, 俊一ja
dc.contributor.alternative笹沼, 博之ja
dc.date.accessioned2015-06-23T07:12:15Z-
dc.date.available2015-06-23T07:12:15Z-
dc.date.issued2015-06-18ja
dc.identifier.issn0305-1048ja
dc.identifier.urihttp://hdl.handle.net/2433/198501-
dc.descriptionシムケ免疫不全・骨形成不全症の原因遺伝子SMARCAL1は、DNA二重鎖切断損傷からゲノムを守る. 京都大学プレスリリース. 2015-06-23.ja
dc.description.abstractSmarcal1 is a SWI/SNF-family protein with an ATPase domain involved in DNA-annealing activities and a binding site for the RPA single-strand-DNA-binding protein. Although the role played by Smarcal1 in the maintenance of replication forks has been established, it remains unknown whether Smarcal1 contributes to genomic DNA maintenance outside of the S phase. We disrupted the SMARCAL1 gene in both the chicken DT40 and the human TK6 B cell lines. The resulting SMARCAL1(-/-) clones exhibited sensitivity to chemotherapeutic topoisomerase 2 inhibitors, just as nonhomologous end-joining (NHEJ) null-deficient cells do. SMARCAL1(-/-) cells also exhibited an increase in radiosensitivity in the G1 phase. Moreover, the loss of Smarcal1 in NHEJ null-deficient cells does not further increase their radiosensitivity. These results demonstrate that Smarcal1 is required for efficient NHEJ-mediated DSB repair. Both inactivation of the ATPase domain and deletion of the RPA-binding site cause the same phenotype as does null-mutation of Smarcal1, suggesting that Smarcal1 enhances NHEJ, presumably by interacting with RPA at unwound single-strand sequences and then facilitating annealing at DSB ends. SMARCAL1(-/-)cells showed a poor accumulation of Ku70/DNA-PKcs and XRCC4 at DNA-damage sites. We propose that Smarcal1 maintains the duplex status of DSBs to ensure proper recruitment of NHEJ factors to DSB sites.ja
dc.format.mimetypeapplication/pdfja
dc.language.isoengja
dc.publisherOxford University Pressja
dc.rights© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.ja
dc.rightsThis is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.ja
dc.titleSmarcal1 promotes double-strand-break repair by nonhomologous end-joining.ja
dc.type.niitypeJournal Articleja
dc.identifier.ncidAA00760269ja
dc.identifier.jtitleNucleic acids researchja
dc.identifier.volume43ja
dc.identifier.issue13ja
dc.identifier.epage6359ja
dc.relation.doi10.1093/nar/gkv621ja
dc.textversionpublisherja
dc.identifier.artnum6372ja
dc.identifier.pmid26089390ja
dc.relation.urlhttps://www.kyoto-u.ac.jp/ja/research-news/2015-06-23ja
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