Analysis of functional dynamics of membrane proteins in different membrane environments
| Project/Area Number |
18H02393
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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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| Review Section |
Basic Section 43020:Structural biochemistry-related
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| Research Institution | Yokohama City University |
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Principal Investigator |
Takahashi Hideo 横浜市立大学, 生命医科学研究科, 教授 (60265717)
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| Co-Investigator(Kenkyū-buntansha) |
竹内 恒 国立研究開発法人産業技術総合研究所, 生命工学領域, 研究グループ長 (20581284)
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| Project Period (FY) |
2018-04-01 – 2022-03-31
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| Project Status |
Completed (Fiscal Year 2021)
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| Budget Amount *help |
¥17,290,000 (Direct Cost: ¥13,300,000、Indirect Cost: ¥3,990,000)
Fiscal Year 2021: ¥3,380,000 (Direct Cost: ¥2,600,000、Indirect Cost: ¥780,000)
Fiscal Year 2020: ¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2019: ¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2018: ¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
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| Keywords | NMR / 膜タンパク質 / 界面活性剤 / 脂質 / 酵素 |
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| Outline of Final Research Achievements |
In this study, we showed that the enzymatic activity of a rhomboid protease is regulated by the alkyl chain length and the properties of hydrophilic head groups of solubilized detergents. And it was found that the enzymatic activity is inversely correlated with the thermal stability of the molecule, which inferred that the internal dynamics of the rhomboid protease affects the enzymatic activities. Using microbial rhodopsin derived from thermophilic eubacteria, we performed a systematic analysis of the thermal stability in different membrane mimetics including bicelles and nanodiscs, which provides us a useful index of choices of membrane environments for functional and structural analyses of membrane proteins. Furthermore, NMR analysis of the rhodopsin in different environments revealed that the environmental difference induces local structural changes that affect the thermal stability of the molecule.
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| Academic Significance and Societal Importance of the Research Achievements |
膜タンパク質は高い疎水性を有し、水溶液中に単離することが困難であるため、その研究を進めるうえでは界面活性剤などの膜様物質とともに可溶化することが行われる。しかしながら、選択した膜様環境において、構造・機能・安定性がどのように維持されるかという点は、学術的にも、創薬研究や分子工学研究などの応用研究を展開する上でも重要な問題となる。本研究で得られた知見は、他の膜タンパク質研究を進めるうえでの指標となるばかりでなく、周辺環境が膜タンパク質に及ぼす影響を原子レベルで理解するための端緒となる研究成果であるといえる。
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Report
(5 results)
Research Products
(43 results)
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[Journal Article] Cooperative interactions facilitate stimulation of Rad51 by the Swi5-Sfr1 auxiliary factor complex.2020
Author(s)
Argunhan B, Sakakura M, Afshar N, Kurihara M, Ito K, Maki T, Kanamaru S, Murayama Y, Tsubouchi H, Takahashi M, Takahashi H, Iwasaki H.
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Journal Title
DOI
NAID
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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[Journal Article] Aromatic 19F-13C TROSY: a background-free approach to probe biomolecular structure, function, and dynamics2019
Author(s)
Boeszoermenyi A, Chhabra S, Dubey A, Radeva D. L, Burdzhiev N. T, Chanev C. D, Petrov O. I, Gelev V. M, Zhang M, Anklin C, Kovacs H, Wagner G, Kuprov I, Takeuchi K, Arthanari H.
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Journal Title
Nat. Methods
Volume: 16
Pages: 333-340
DOI
Related Report
Peer Reviewed / Int'l Joint Research
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