Lysines 3241 and 3260 of DNA-PKcs are important for genomic stability and radioresistance.

• Material Type: 博士論文
• ISSN: 0006-291X
• Title: Lysines 3241 and 3260 of DNA-PKcs are important for genomic stability and radioresistance.
• Volume: 477 2
• Author/Editor: Mori, Eiichiro; Davis, Anthony J.; Hasegawa, Masatoshi; Chen, David J.
• Author Heading: Mori, Eiichiro; Davis, Anthony J.; Hasegawa, Masatoshi; Chen, David J.
• Publication, Distribution, etc.: Elsevier
• Publication Date: 2016-08-19; 477 2
• Publication Date (W3CDTF): 2016-08-19
• Alternative Title: DNA-PKcsのリジン3241と3260はゲノムの安定性と放射線抵抗性に重要である
• Periodical title: Biochemical and biophysical research communications Vol. No. p.- (2016 Aug)
• Degree grantor/type: 奈良県立医科大学
• Date Granted: 2017-06-28
• Date Granted (W3CDTF): 2017-06-28
• Dissertation Number: 甲第670号
• Degree Type: 博士（医学）
• Conferring No. (Dissertation): 甲第670号
• Text Language Code: eng
• Subject Heading: DNA double-strand breaks; Non-homologous end-joining; Acetylation; DNA-PKcs
• Target Audience: 一般
• Note (General): type:Thesis; DNA-dependent protein kinase (DNA-PK) is a serine/threonine kinase that plays an essential role in the repair of DNA double-strand breaks (DSBs) in the non-homologous end-joining (NHEJ) pathway. The DNA-PK holoenzyme consists of a catalytic subunit (DNA-PKcs) and DNA-binding subunit (Ku70/80, Ku). Ku is a molecular sensor for double-stranded DNA and once bound to DSB ends it recruits DNA-PKcs to the DSB site. Subsequently, DNA-PKcs is activated and heavily phosphorylated, with these phosphorylations modulating DNA-PKcs. Although phosphorylation of DNA-PKcs is well studied, other post-translational modifications of DNA-PKcs are not. In this study, we aimed to determine if acetylation of DNA-PKcs regulates DNA-PKcs-dependent DSB repair. We report that DNA-PKcs is acetylated in vivo and identified two putative acetylation sites, lysine residues 3241 and 3260. Mutating these sites to block potential acetylation results in increased radiosensitive, a slight decrease in DSB repair capacity as assessed by γH2AX resolution, and increased chromosomal aberrations, especially quadriradial chromosomes. Together, our results provide evidence that acetylation potentially regulates DNA-PKcs.; 博士（医学）・甲第670号・平成29年6月28日; Copyright © 2016 Elsevier Inc. All rights reserved.; identifier:Biochemical and biophysical research communications Vol.477 No.2 p.235-240 (2016 Aug); identifier:0006291X; identifier:http://ginmu.naramed-u.ac.jp/dspace/handle/10564/3342; identifier:Biochemical and biophysical research communications Vol. No. p.- (2016 Aug), 477(2): 235-240
• DOI: info:doi/10.1016/j.bbrc.2016.06.048; https://doi.org/info:doi/10.1016/j.bbrc.2016.06.048
• Persistent ID (NDL): info:ndljp/pid/10402820; https://dl.ndl.go.jp/pid/10402820
• Collection: 障害者向け資料
• Collection (Materials For Handicapped People:1): テキストデータ
• Collection (particular): 国立国会図書館デジタルコレクション > デジタル化資料 > 博士論文; https://dl.ndl.go.jp/collections/A00014
• Acquisition Basis: 博士論文（自動収集）
• Date Accepted (W3CDTF): 2017-08-02T04:31:34+09:00
• Format (IMT): application/pdf
• Access Restrictions: 国立国会図書館内限定公開
• Service for the Digitized Contents Transmission Service: 図書館・個人送信対象外
• Availability of remote photoduplication service: 可
• Periodical Title (URI): http://hdl.handle.net/10564/3342
• Data Provider (Database): 国立国会図書館 : 国立国会図書館デジタルコレクション; https://dl.ndl.go.jp

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