2013 Fiscal Year Final Research Report
Mechanism of histone dimethylation regulating DNA damage response
| Project/Area Number |
23310038
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Risk sciences of radiation/Chemicals
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| Research Institution | Nagasaki University |
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Principal Investigator |
SUZUKI Keiji 長崎大学, 原爆後障害医療研究所, 准教授 (00196809)
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| Project Period (FY) |
2011-04-01 – 2014-03-31
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| Keywords | 放射線 / DNA / クロマチン / ヒストン / メチル化 |
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| Research Abstract |
To secure genome integrity of the cells DNA damage signals are amplified and persists, if DNA double strand breaks are remained. This study demonstrated that , G9a, a histone H3 dimethylase, is involved in persisted DNA damage signal amplification. G9a was found to be relocated to the chromatin regions harboring DNA damage, and it executed dimethylation of histone H3 at Lysine 9. Dimethylated histone H3 at Lysine 9 was recognized by 53BP1 through its so-called Tudor domain, thereby amplified 53BP1 foci formation was maintained. The study indicated that dimethylation of histone H3 at Lysine 9 by recruted G9a to DNA damage sites is essential for the persistence of amplified DNA damage signals.
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Research Products
(11 results)
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[Journal Article] Singnificance of p53-binding protein 1 (53BP1) expression in thyroid papillary microcarcinoma : association with BRAFV600E mutation status2013
Author(s)
Mussazhanova Z, Matsuda K, Naruke Y, Mitsutake N, Stanojevic B, Rogounovitch T, Saenko V, Suzuki K, Nishihara E, Hirokawa M, Ito M, Nakashima M
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Journal Title
Histopathology
Volume: 63
Pages: 726-734
DOI
Peer Reviewed
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