Accumulation of proteins utilizing the ring-structure formed by alpha6 and alpha7 subunits of human 20S proteasome
| Project/Area Number |
26460051
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Physical pharmacy
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| Research Institution | Meijo University |
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Principal Investigator |
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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 |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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| Keywords | タンパク質 / 集積化 / プロテアソーム / リング / バイオ素子 / 集積 |
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| Outline of Final Research Achievements |
The aim of this study is accumulation of proteins based on the homo-double ring formed by alpha7 subunits of human 20S proteasome. GFP, employed as model protein, was fused at N- or C-terminus of alpha7. Resultant proteins did not show ring-formation. Therefore, hetero-ring formation using alpha6 subunit fused with GFP at the N- or C-terminus was attempted. GFP-alpha6 formed hetero-ring efficiently with monomeric form of alpha7, but did not with alpha7 homo-double ring. On the other hand, alpha6-GFP easily formed hetero-ring both with monomeric or oligomeric alpha7. Moreover, GFP-alpha6-GFP formed hetero-ring with monomeric alpha7, indicating that such fusion is effective for higher accumulation of proteins on the ring.
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Report
(4 results)
Research Products
(7 results)
