2013 Fiscal Year Final Research Report
Mechanism underlying difference between transmissible and nontransmissible amyloids
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 |
Research Field |
Structural biochemistry
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Research Institution | Tokyo Institute of Technology |
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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Keywords | 酵母プリオン |
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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Research Products
(19 results)
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[Journal Article] The interaction of Hsp104 with yeast prion Sup35 as analyzed by fluorescence cross-correlation spectroscopy2013
Author(s)
Ohta, S., Kawai-Noma, S., Kitamura, A., Pack, C-G., Kinjo, M. & Taguchi, H.
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Journal Title
Biochem. Biophys. Res. Commun.
Volume: 442
Pages: 28-32
Peer Reviewed
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[Journal Article] Experimental study on the mechanism underlying the anti-aggregation function of a group3LEA peptide2013
Author(s)
Yamakawa, K., Furuki, T., Furuta, T., Hatanaka, R., Kikawada, T., Niwa, T. Taguchi, H. Furusawa H., Okahata, Y., and Sakurai, M.
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Journal Title
Cryobiol. Cryotechnol.
Volume: 59
Pages: 95-99
Peer Reviewed
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[Journal Article] Biomolecular Robotics for Chemomechanically Driven Guest Delivery Fueled by Intracellular ATP2013
Author(s)
Biswas, S., Kinbara, K., Niwa, T., Taguchi, H., Ishii, N., Watanabe, S., Miyata, K., Kataoka, K., Aida, T.
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Journal Title
Nature Chemistry
Volume: 5
Pages: 613-620
Peer Reviewed
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[Journal Article] Nano-scale alignment of proteins on a flexible DNA back-bone2012
Author(s)
Nojima, T., Konno, H., Kodera, N., Seio, K., Taguchi, H. and Yoshida, M.
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Journal Title
PLoS One
Volume: 7
Pages: e52534
Peer Reviewed
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