| Project/Area Number |
25282235
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Biomolecular chemistry
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| Research Institution | Suntory Foundation for Life Sciences |
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Principal Investigator |
SHIMAMOTO Keiko 公益財団法人サントリー生命科学財団, その他部局等, その他 (70235638)
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| Co-Investigator(Renkei-kenkyūsha) |
MIURA Kaoru (Nomura Kaoru) (公益財団法人)サントリー生命科学財団, 生物有機科学研究所, 研究員 (90353515)
NISHIYAMA Ken-ichi 岩手大学, 農学部, 教授 (80291334)
MURATA Michio 大阪大学, 大学院理学研究科, 教授 (40183652)
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥18,590,000 (Direct Cost: ¥14,300,000、Indirect Cost: ¥4,290,000)
Fiscal Year 2015: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
Fiscal Year 2014: ¥7,150,000 (Direct Cost: ¥5,500,000、Indirect Cost: ¥1,650,000)
Fiscal Year 2013: ¥8,320,000 (Direct Cost: ¥6,400,000、Indirect Cost: ¥1,920,000)
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| Keywords | 糖脂質 / 膜挿入 / 膜タンパク質 / 糖鎖合成 / 生体膜 / 生合成基質 / シャペロン / 糖鎖 |
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| Outline of Final Research Achievements |
We previously reported an integration factor in the inner membrane of E. coli, named MPIase (membrane protein integrase) is a glycolipid composed of diacylglycerol and a glycan chain of three acetylated aminosugars linked through pyrophosphate. MPIase is essential for membrane protein integration and acts like an enzyme. In this study, we showed that O-acetyl groups in the glycan and a phosphate group are required for its activity. NMR experiments indicated the interaction between the acetyl groups of MPIase and the substrate peptide. Based on these results, we propose a plausible mode of action, in which a glycan chain of MPIase captures a substrate to prevent aggregation. Moreover, we synthesized a trisaccharide unit of MPIase to reveal a minimum active structure.
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