| Project/Area Number |
25882050
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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 |
Biomolecular chemistry
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| Research Institution | High Energy Accelerator Research Organization |
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Principal Investigator |
YUMOTO Fumiaki 大学共同利用機関法人高エネルギー加速器研究機構, 物質構造科学研究所, 特任准教授 (30360150)
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| Project Period (FY) |
2013-08-30 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
Fiscal Year 2014: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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| Keywords | LRH-1 / X線結晶構造解析 / X線小角散乱解析 / 分子認識 / 結晶化 / X線溶液散乱解析 |
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| Outline of Final Research Achievements |
LRH-1 plays an essential role in early development as it is expressed in embryonic stem cells. It is a transcription factor expressed in liver, pancreas, and ovary to regulate gene expressions. In addition to the biological aspect, it has been recognized as a drug target because the receptor is involved in multiple cancer developments. Full-length LRH-1 and N-terminal region-truncated LRH-1 were produced in E. coli and complexes of the protein-DNA duplex were further purified by gel filtration after elution from Ni-NTA column. The complex formation with DNA was critical to handle the sample for structural study and for biochemical characterization. LRH-1-DNA-peptide ternary complex was also prepared. The samples have been tested in small angle X-ray scattering and crystallization with the samples. The results suggested that the both LRH-1 molecules such as full-length and N-terminal truncated version had “bar” type shape.
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