Proteomics analysis of hEPC1 polycomb protein complex in DNA damaged repair.
| Project/Area Number |
15370078
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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 |
Molecular biology
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| Research Institution | HIROSHIMA UNIVERSITY |
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Principal Investigator |
IKURA Tsuyoshi Hiroshima Univ., Research Institute for Radiation Biology and Medicine, Research Associate, 原爆放射線医科学研究所, 助手 (70335686)
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| Co-Investigator(Kenkyū-buntansha) |
KAMIYA Kenji Hiroshima Univ., Research Institute for Radiation Biology and Medicine, Professor, 原爆放射線医科学研究所, 教授 (60116564)
MASUDA Yuji Hiroshima Univ., Research Institute for Radiation Biology and Medicine, Research Associate, 原爆放射線医科学研究所, 助手 (30273866)
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| Project Period (FY) |
2003 – 2004
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| Project Status |
Completed (Fiscal Year 2004)
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| Budget Amount *help |
¥15,300,000 (Direct Cost: ¥15,300,000)
Fiscal Year 2004: ¥7,400,000 (Direct Cost: ¥7,400,000)
Fiscal Year 2003: ¥7,900,000 (Direct Cost: ¥7,900,000)
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| Keywords | Enhancer of polycomb / TIP60 complex / Histone H2AX / hEPC1 complex / MS analysis / Acetylation / histone acetylase enzyme / Dynamics of protein complex / Enhancer of polycomb(hEPC1) / 複合体ダイナミクス / hEPC複合体 / 複合体のダィナミクス / TIP60 |
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| Research Abstract |
Eukaryotic genome is the tightly packed into the chromatin, a hierarchically organized complex of DNA and histone and nonhistone proteins. This packing represents a common obstacle for most of the DNA functions. Recently, we revealed that TIP60 histone acetylase complex involved in DNA repair and apoptosis. However, it remains unknown how TIP60 complex involves in DNA repair. To better understand the mechanism of TIP60 complex in DNA repair, TIP60 complex purifies from chromatin soluble fraction after DNA damage. As a result, enhancer of polycomb (hEPC1), the component of TIP60 complex, dissociated with the TIP60 complex. In order to clarify the role of hEPC1 in DNA repair,
We purified the hEPC1 from HeLa after induction of DNA damage. hEPC1 was included in multiple protein complex. MS/MS analysis indicated that kinase, metyltransferase enzyme, histone H2AX, TIP60 histone acetylase and ubiquitin related proteins were identified as a component of hEPC1 complex. Metyltransferase activity was observed. In addition, Histone H2AX is phosphorylated after DNA damage. The phosphorylation of H2AX was inhibited in HeLa cells expressing siEPC RNA suggested that the hEPC1 complex includes kinase domain.
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Report
(3 results)
Research Products
(33 results)
