| Project/Area Number |
24657070
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Single-year Grants |
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| Research Field |
Structural biochemistry
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| Research Institution | Tokyo Institute of Technology |
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Principal Investigator |
TAGUCHI Hideki 東京工業大学, 生命理工学研究科, 教授 (40272710)
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2013: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2012: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | 酵母プリオン / プリオン / アミロイド / 出芽酵母 |
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| Research Abstract |
The yeast prions are protein-based heritable elements, such as [PSI+]. N-terminal domain of Sup35 (Sup35N), the amyloids of which is the [PSI+] determinant, contains a glutamine and asparagine (Q/N)-rich sequence. When Sup35N is replaced with a polyglutamine (polyQ) stretch the polyQ-replaced Sup35 (polyQ-Sup35) forms amyloids in cells, but cannot be inherited as a prion. Since the mechanism underlying the difference remains to be elucidated, we explored the dynamics of both amyloids in single living cells. Single-cell imaging revealed that the visible large aggregates of polyQ-Sup35 fused with GFP maintained their sizes during cell growth. In addition, polyQ-Sup35 had an increased tendency to form aggregates compared to Sup35N. Then we searched peptides that convert polyQ-Sup35 from nontransmissible to transimissible amyloids when flanked with polyQ region, and identified at least 20 prionized peptides. PolyQ-Sup35 attached with the prionized peptide diffused faster in cells.
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