Analysis of unidentified truncation mechanism of misfolded proteins
| Project/Area Number |
25440058
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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 |
Functional biochemistry
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| Research Institution | Institute of Physical and Chemical Research |
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Principal Investigator |
Hosomi Akira 国立研究開発法人理化学研究所, 糖鎖代謝学研究チーム, 協力研究員 (60525864)
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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 |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2015: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | 酵母 / 小胞体関連分解 / エンドペプチダーゼ / ERAD / glycoprotein / yeast / 異常タンパク質 / タンパク質分解 |
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| Outline of Final Research Achievements |
Misfolded proteins are degraded by proteasome in ER-associated degradation (ERAD). However, our previous study suggested that unidentified protease cleaves CPY* (carboxypeptidase Y mutant), which is a major ERAD model substrate, in budding yeast. To clarify the mechanism of the cleavage, we analyzed CPY* intermediates. Our study demonstrated that 50k and 30k intermediates were generated and cleavage site for 50k intermediate is located in 400-404 amino acid residues.
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Report
(4 results)
Research Products
(4 results)
