Structural analysis of histone proteins extracted from DNA damaged cells using circular dichroism spectroscopy
Project/Area Number |
15K16130
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Risk sciences of radiation and chemicals
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Research Institution | Hiroshima University (2016) Japan Atomic Energy Agency (2015) |
Principal Investigator |
Izumi Yudai 広島大学, 放射光科学研究センター, 助教 (20595772)
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Project Period (FY) |
2015-04-01 – 2017-03-31
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Project Status |
Completed (Fiscal Year 2016)
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Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2016: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2015: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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Keywords | DNA損傷応答 / ヒストン / 円二色性 / 翻訳後修飾 / 放射光 / 放射線生物学 |
Outline of Final Research Achievements |
In an attempt to investigate structural alterations of histone proteins induced by DNA damage responses, we measured circular dichroism spectra of histones extracted from DNA-damaged cells. We revealed that DNA damage response increases α-helix structure in histone H2A-H2B, but decreases that in histone H3-H4. Since different structural alterations were observed in H2A-H2B and H3-H4, it is suggested that the structural alterations of histones are caused by the several pathways. Interestingly, these altered structures persisted for at least 24 hours. These structural alterations would play an important role in DNA damage responses, such as DNA damage repair pathways.
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Report
(3 results)
Research Products
(14 results)
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[Journal Article] Structural transition from β-strand and turn to α-helix in histone H2A-H2B induced by DNA damage response2016
Author(s)
Y. Izumi, K. Fujii, F. Wien, C. Houee-Levin, S. Lacombe, D. Salado-Leza, E. Porcel, R. Masoud, S. Yamamoto, M. Refegiers, M. -A. Herve du Penhoat, and A. Yokoya
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Journal Title
Biophysics Journal
Volume: 111
Issue: 1
Pages: 69-78
DOI
Related Report
Peer Reviewed / Int'l Joint Research / Acknowledgement Compliant
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