Regulaion of epigenome by the SUMO and ubiquitin modification systems
| Project/Area Number |
23616004
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
epigenetics
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| Research Institution | Kumamoto University |
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Principal Investigator |
SAITOH Hisato 熊本大学, 自然科学研究科, 教授 (50211925)
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| Co-Investigator(Renkei-kenkyūsha) |
SUGASAWA Kaoru 神戸大学, バイオシグナル研究センター, 教授 (70202124)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2013: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2012: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2011: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | SUMO / ユビキチン / TDG / RNF4 / 塩基除去修復 / DNA脱メチル化 / 細胞周期 / PML / 脱メチル化 / 翻訳後修飾 / クロマチン / 細胞分化 / 遺伝子発現 |
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| Research Abstract |
Thymine DNA glycosylase (TDG) is a base excision repair (BER) enzyme that interacts with the small ubiquitin-related modifier (SUMO)-targeted ubiquitin E3 ligase RNF4 and functions in the active DNA demethylation pathway. Here we found that the majority of TDG was SUMOylated in cells undergoing mitosis, while both SUMOylated and non-modified TDG were eliminated in cells arrested at S phase. In vitro and in vivo binding analyses revealed that TDG interacted with RNF4 in a SUMOylation-independent manner. In RNF4-depleted cells, both forms of TDG were efficiently degraded, suggesting that RNF4 was not the primary E3 ligase for controlling TDG stability. Our findings would not only be important for understanding posttranslational regulation of TDG but also provide implications for the TDG-RNF4 interaction in BER-driven active DNA demethylation during cell cycle progression.
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Report
(4 results)
Research Products
(56 results)
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[Journal Article] SUMO-modification and elimination of the active DNA demethylation enzyme TDG in cultured human cells2014
Author(s)
Moriyama, T., Fujimitsu, Y., Yoshikai, Y., Sasano, T., Yamada, K., Murakami, M., Urano, T., Sugasawa, K. and Saitoh, H.
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Journal Title
Biochem Biophys Res Commun
Volume: 447
Pages: 419-424
DOI
Related Report
Peer Reviewed / Open Access
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[Journal Article] Spectomycin B1 as a Novel SUMOylation Inhibitor That Directly Binds to SUMO E22013
Author(s)
Hirohama M, Kumar A, Fukuda I, Matsuoka S, Igarashi Y, Saitoh H, Takagi M, Shin-ya K, Honda K, Kondoh Y, Saito T, Nakao Y, Osada H, Zhang KY, Yoshida M, Ito A
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Journal Title
ACS Chem Biol.
Volume: 8
Pages: 2635-2642
DOI
Related Report
Peer Reviewed
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[Journal Article] Activation of the SUMO modification system is required for the accumulation of RAD51 at sites of DNA damage.2013
Author(s)
Shima H, Suzuki H, Sun J, Kono K, Shi L, Kinomura A, Horikoshi Y, Ikura T, Ikura M, Kanaar R, Igarashi K, Saitoh H, Kurumizaka H, Tashiro S
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Journal Title
Journal Cell Science
Volume: 126
Pages: 5284-5292
DOI
Related Report
Peer Reviewed
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