Understanding the molecular mechanism of co-translational oxidative folding in the ER
Project/Area Number |
17H06521
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Research Category |
Grant-in-Aid for Research Activity Start-up
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Allocation Type | Single-year Grants |
Research Field |
Biophysics
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Research Institution | Kwansei Gakuin University (2018) Tohoku University (2017) |
Principal Investigator |
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Project Period (FY) |
2017-08-25 – 2019-03-31
|
Project Status |
Completed (Fiscal Year 2018)
|
Budget Amount *help |
¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
Fiscal Year 2018: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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Keywords | 無細胞タンパク質合成系 / セミインタクト細胞 / PDIファミリー / ジスルフィド結合 / 新生鎖 |
Outline of Final Research Achievements |
In order to provide structural insight into "the mechanism of how oxidative folding occurs co-translationally in the ER", I developed "a monitoring system regarding the reaction of disulfide bond formation of nascent polypeptides". The results indicated that a disulfide bond of the β2m nascent chain is formed in the lumen of the ER during the translation elongation, and disulfide bonds of prolactin, insulin, and BPTI nascent chain are post-translationally formed.
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Academic Significance and Societal Importance of the Research Achievements |
本研究によって、新生鎖のジスルフィド結合形成過程の観察に成功した。本成果は今後、インスリンや免疫グロブリンなどの生物学的、医学的にも重要なタンパク質の立体構造を構築する(フォールディング)機序の解明に繋がると期待できる。フォールディング機序の解明は、ミスフォールディングに起因する神経変性疾患などの予防や発症機構の解明にも繋がり、医学分野への貢献も大いに期待でき非常に意義深い。
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Report
(3 results)
Research Products
(9 results)