Investigation, modification and utilization of the retinal proteins
| Project/Area Number |
15H04363
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | Okayama University |
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Principal Investigator |
Sudo Yuki 岡山大学, 医歯薬学総合研究科, 教授 (10452202)
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| Co-Investigator(Renkei-kenkyūsha) |
TSUKAMOTO Takashi 岡山大学, 大学院医歯薬学総合研究科(薬学系), 助教 (30744271)
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥16,380,000 (Direct Cost: ¥12,600,000、Indirect Cost: ¥3,780,000)
Fiscal Year 2017: ¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2016: ¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2015: ¥7,540,000 (Direct Cost: ¥5,800,000、Indirect Cost: ¥1,740,000)
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| Keywords | 生物物理 / ロドプシン / レチナール / 光遺伝学 / オプトジェネティクス / 生体分子 / 分子機械 / 膜タンパク質 / 光 / イオン輸送 / 分子認識 / 生物・生体工学 / 光操作 |
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| Outline of Final Research Achievements |
Retinal protein, also called "rhodopsin", has a vitamin-A aldehyde as a chromophore. It is widely distributed in the three biological domains (animals, bacteria, archaea), and is responsible for various light-dependent functions. In addition to such biological interests, recently, the new technology called "optogenetics" which is a method for controlling biological activities by light, has been established as a collaborative work with the retinal proteins. In this research, based on the background, we investigated the retinal proteins fundamentally by using various methods. Then we modified the molecular properties to develop the novel optogenetics tools that can be widely utilized for scientific research.
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Report
(4 results)
Research Products
(44 results)
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[Journal Article] Demonstration of a light-driven SO42- transporter and its spectroscopic characteristics2017
Author(s)
Niho A, Yoshizawa S, Tsukamoto T, Kurihara M, Tahara S, Nakajima Y, Mizuno M, Kuramochi H, Tahara T, Mizutani Y, *Sudo Y.
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Journal Title
J. Am. Chem. Soc.
Volume: 139
Issue: 12
Pages: 4376-4389
DOI
NAID
Related Report
Peer Reviewed / Acknowledgement Compliant
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[Journal Article] X-ray crystallographic structure of thermophilic rhodopsin: implications for high thermal stability and optogenetic function2016
Author(s)
Tsukamoto T, Mizutani K, Hasegawa T, Takahashi M, Honda N, Hashimoto N, Shimono K, Yamashita K, Yamamoto M, Miyauchi S, Takagi S, Hayashi S, Murata T, Sudo Y.
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Journal Title
J. Biol. Chem.
Volume: in press
Issue: 23
Pages: 12223-12232
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Journal Article] Factors affecting the stability and performance of ionic liquid-based planar transient photodetectors2015
Author(s)
*Dalgleish, S., Reissig, L., Hu, L., Matsushita, M.M., Sudo, Y., & *Awaga, K.
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Journal Title
Langmuir
Volume: 印刷中
Issue: 18
Pages: 5235-5243
DOI
Related Report
Peer Reviewed
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[Journal Article] Atomistic design of microbial opsin-based blue-shifted optogenetics tools2015
Author(s)
Kato HE, Kamiya M, Sugo S, Ito J, Taniguchi R, Orito A, Hirata K, Inutsuka A,Yamanaka A, Maturana AD, Ishitani R, Sudo Y, Hayashi S, Nureki O
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Journal Title
Nat Commun
Volume: 6
Issue: 1
Pages: 7177-7177
DOI
NAID
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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