Elucidation of nucleosome structural changes based on histone modifications
| Project/Area Number |
24370052
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | The University of Tokyo |
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Principal Investigator |
Horikoshi Masami 東京大学, 分子細胞生物学研究所, 准教授 (70242089)
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| Project Period (FY) |
2012-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥18,330,000 (Direct Cost: ¥14,100,000、Indirect Cost: ¥4,230,000)
Fiscal Year 2014: ¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2013: ¥6,110,000 (Direct Cost: ¥4,700,000、Indirect Cost: ¥1,410,000)
Fiscal Year 2012: ¥7,800,000 (Direct Cost: ¥6,000,000、Indirect Cost: ¥1,800,000)
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| Keywords | ヒストンシャペロン / ヌクレオソーム / 化学修飾 / 構造変換 / ヌクレオソームアセンブリー / ヌクレオソームディスアセンブリー / ヒストン / ヒストンバリアント |
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| Outline of Final Research Achievements |
We used a histone-GLibrary that encompasses the nucleosomal DNA entry/exit site to show that six residues form a surface on the structured nucleosome core and regulate H3-K36me3. We also found an interaction between Jhd2 and H2A. Two H2A residues serve as a binding site for Jhd2 and mediate its chromatin association and H3K4 demethylase functions. We described a method to discriminate between the functions of a common subunit in different multisubunit complexes. A common subunit in a multisubunit complex is genetically fused to a subunit that is specific to that complex and point mutated. The resulting phenotype(s) identify the specific function(s) of the subunit in that complex only. We proposed an innovative concept for evolutionary analysis that does not require an outer group. This approach utilizes the similarity in intramolecular direct repeats as an evolutionary measure revealing the degree of similarity between the present offspring genes and their ancestors.
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Report
(5 results)
Research Products
(18 results)
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[Journal Article] Interaction of the Jhd2 H3K4 demethylase with chromatin is promoted by histone H2A surfaces and restricted by H2B ubiquitylation2015
Author(s)
F.Huang, S.Ramakrishnan, C.Pflueger, T.J.Parnell, M.M.Kasten, S.L.Currie, N.Bhachech, M.Horikoshi, B.J.Graves, S.Bhaskara, B.R.Cairns & M.B.Chandrasekharan
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Journal Title
J.Biol.Chem.
Volume: 290
Issue: 48
Pages: 28760-28777
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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