| Project/Area Number |
16K14904
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Applied biochemistry
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| Research Institution | Toyama Prefectural University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
IKUSHIRO SHINICHI 富山県立大学, 工学部, 准教授 (50244679)
YASUDA KAORI 富山県立大学, 工学部, 助教 (70707231)
NISHIKAWA MIYU 富山県立大学, 工学部, 嘱託研究員 (90749805)
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| Research Collaborator |
MANO HIROKI
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| Project Period (FY) |
2016-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2017: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2016: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | ルシフェラーゼ / ビタミンD受容体 / シグナル伝達 / 高感度検出系 / キメラ酵素 / 酵素 / GFP / ビタミンD |
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| Outline of Final Research Achievements |
A biosensor to detect vitamin D receptor (VDR) ligand with high sensitivity was developed using the technology of the split-type luciferase.The N-terminal portion (LucN) and C-terminal portion (LucC) of the split luciferase was fused to N-terminus and C-terminus of the VDR-ligand-binding domain (LBD), respectively. The binding of active form of vitamin D to LBD in the biosensor induces a conformational change of the biosensor. Cosequently, the LucN and LucC positions are contiguous to increase luciferase activity. We also successfully developed a biosensor consisting of LucN with additiona peptide and LBD-LucC. When the ligand binds to LBD, the interaction between the two molecules is enhanced, and then the luciferase activity is increased.
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