Project for revealing the mechanism of the histone exchange activity of testis specific histone variant H2A.B.
| Project/Area Number |
15H06691
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| Research Category |
Grant-in-Aid for Research Activity Start-up
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| Allocation Type | Single-year Grants |
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| Research Field |
Genome biology
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| Research Institution | Waseda University |
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Principal Investigator |
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| Project Period (FY) |
2015-08-28 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
Fiscal Year 2016: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2015: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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| Keywords | クロマチン / エピジェネティクス / ヌクレオソーム / ヒストン / H2A.B / ヒストンバリアント / ゲノム |
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| Outline of Final Research Achievements |
The purpose of this project is to reveal the mechanism of the histone exchange activity of testis specific histone variant H2A.B. Previously, I found that the H2A.B-H2B dimers are efficiently exchanged with the canonical H2A-H2B dimers within the nucleosome. In this project, I studied the mechanism by which histone H2A.B-H2B dimers are exchanged with the canonical H2A-H2B dimers. To do so, biochemical, structural, and cell biological analyses were performed. In biochemical analysis, the domain responsible for the histone exchange activity of H2A.B was determined by the swapping mutational analysis. To reveal the function of this domain in cells, fluorescence recovery after photobleaching assay was performed using cells expressing GFP-tagged H2A.B. I obtained structural information for the exchange-intermediate nucleosomes containing H2A.B by X-ray crystallography and small angle X-ray scattering methods.
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Report
(3 results)
Research Products
(9 results)
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[Journal Article] Polymorphism of apyrimidinic DNA structures in the nucleosome.2017
Author(s)
Osakabe, A., Arimura, Y., Matsumoto, S., Horikoshi, N., Sugasawa, K., Kurumizaka, H.
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Journal Title
Scientific Reports
Volume: 7
Issue: 1
Pages: 41783-41783
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Presentation] Cancer-associated histone mutations affect the structure and stability of the nucleosome2016
Author(s)
Yasuhiro Arimura, Mamiko Noda, Risa Fujita, Masae Ikura, Masaaki Sugiyama, Hiroshi Kimura, Tsuyoshi Ikura, and Hitoshi Kurumizaka,
Organizer
the 4th Cold Spring Harbor Asia conference on Chromatin, Epigenetics and Transcription
Place of Presentation
Suzhou, China
Year and Date
2016-05-09
Related Report
Int'l Joint Research
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