Application of eicosapentaeonic acid-containing phospholipids as a lipophilic protein chaperone
| Project/Area Number |
26660065
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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 microbiology
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| Research Institution | Kyoto University |
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Principal Investigator |
Kawamoto Jun 京都大学, 化学研究所, 助教 (90511238)
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| Co-Investigator(Renkei-kenkyūsha) |
KURIHARA Tatsuo 京都大学, 化学研究所, 教授 (70243087)
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | 低温菌 / エイコサペンタエン酸 / Outer membrane vesicle / Shewanella / リン脂質 / 特殊環境微生物 / 高度不飽和脂肪酸 / 長鎖多価不飽和脂肪酸 |
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| Outline of Final Research Achievements |
Eicosapentaenoic acid (EPA), one of polyunsaturated fatty acids, has various beneficial effects on human health. EPA is naturally found as an acyl chain of membrane phospholipids and changes the physicochemical properties of the membrane, such as the thickness, elasticity, permeability, and fluidity, to modulate functions of membrane proteins. In this study, we focused on the membrane protein production of an EPA-less mutant of a psychrotrophic EPA-producing bacterium, Shewaenlla livingstonensis Ac10, which is isolated from Antarctic seawater and inducibly produces EPA-containing phospholipids at low temperatures. We found that, in the EPA-less mutant, a specific membrane protein was exported to the extracellular region via membrane vesicle production, suggesting that the defect of EPA facilitates a protein unfolding of specific proteins and induces the protein secretion pathway.
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Report
(4 results)
Research Products
(5 results)
