Elucidation of mechanism for conformational change and protein folding of the group 2 chaperonin
Project/Area Number |
21370067
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Biophysics
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Research Institution | Tokyo University of Agriculture and Technology |
Principal Investigator |
YOHDA Masafumi 東京農工大学, 大学院・工学研究院, 教授 (50250105)
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Project Period (FY) |
2009 – 2011
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Project Status |
Completed (Fiscal Year 2011)
|
Budget Amount *help |
¥18,850,000 (Direct Cost: ¥14,500,000、Indirect Cost: ¥4,350,000)
Fiscal Year 2011: ¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2010: ¥5,720,000 (Direct Cost: ¥4,400,000、Indirect Cost: ¥1,320,000)
Fiscal Year 2009: ¥7,540,000 (Direct Cost: ¥5,800,000、Indirect Cost: ¥1,740,000)
|
Keywords | シャペロン / シャペロニン / フォールディング / 構造変化 / 古細菌 / ストップトフロー / ストップドフロー |
Research Abstract |
To elucidate detailed conformational change and protein folding mechanism of the group 2 chaperonin(CPN), we have performed kinetic studies of conformational change by stopped-flow fluorometry, stopped-flow small angle X-ray scattering and Diffracted X-ray Tracking. The results have shown that the conformational change is biphasic and the latter includes the rotational motion of the ring. In addition, we constructed and characterize asymmetric ring complex that consists of a wild-type ring and a mutant ring by using circular permutated connected mutants. The results gave an insight on the inter ring communication of CPN.
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Report
(4 results)
Research Products
(73 results)
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[Journal Article] Dimer structure and conformational variability in the N-terminal region of an archaeal small heat shock protein2011
Author(s)
Takeda, K., Hayashi, T., Abe, T., Hirano, Y., Hanazono, Y., Yohda, M., Miki, K.
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Journal Title
J. Struct. Biol
Volume: 174
Pages: 92-99
Related Report
Peer Reviewed
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[Journal Article] StHsp14. 0, a small heat shock protein of Sulfolobus tokodaii strain 7, protects denatured proteins from aggregation in the partially dissociated conformation2011
Author(s)
Abe, T., Oka, T., Nakagome, A., Tsukada, Y., Yasunaga, T., Yohda, M.
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Journal Title
J. Biochem
Volume: 150
Pages: 403-409
Related Report
Peer Reviewed
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[Journal Article] Thermodynamic Characterization of the Interaction between Prefoldin and Group II Chaperonin2010
Author(s)
Sahlan, M., Zako, T., Tai, P. T., Ohtaki, A., Noguchi, K., Maeda, M., Miyatake, H., Dohmae, N., Yohda, M.
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Journal Title
J. Mol. Biol
Volume: 399
Pages: 628-636
Related Report
Peer Reviewed
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[Journal Article] Adaptation of a hyperthermophilic group II chaperonin to relatively moderate temperatures2010
Author(s)
Kanzaki, T., Ushioku, S., Nakagawa, A., Oka, T., Takahashi, K., Nakamura, T., Kuwajima, K., Yamagishi, A., Yohda, M.
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Journal Title
Protein Eng. Des. Se
Volume: 23
Pages: 393-402
Related Report
Peer Reviewed
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[Journal Article] Crystal structures of the lumazine protein from Photobacterium kishitanii in complexes with the authentic chromophore, 6,7-dimethyl-8-(1'-D-ribityl) lumazine, and its analogues, riboflavin and flavin mononucleotide, at high resolution.2010
Author(s)
Sato Y, Shimizu S, Ohtaki A, Noguchi K, Miyatake H, Dohmae N, Sasaki S, Odaka M, Yohda M.
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Journal Title
J Bacteriol. 192
Pages: 127-133
Related Report
Peer Reviewed
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[Journal Article] Characterization of a sHsp of Schizosaccharomyces pombe, SpHsp 15. 8, and the implication of its functional mechanism by comparison with another sHsp2009
Author(s)
Sugino, C., Hirose, M., Tohda, H., Yoshinari, Y., Abe, T., Giga-Hama, Y., Iizuka, R., Shimizu, M., Kidokoro, S., Ishii, N., Yohda, M.
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Journal Title
Proteins
Volume: 74
Pages: 6-17
Related Report
Peer Reviewed
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[Presentation] Mechanism in Conformational Change of Group II Chaperonin2009
Author(s)
Yohda M., Kanzaki T., Masuda R., Sahlan M., Nakagawa A., Oka T., Takahashi K., Maki K., Yebenes H., Valpuesta M., Igarashi K., Kuwajima K.
Organizer
EXPERIMENTAL BIOLOGY 2009
Place of Presentation
New Orleans, USA
Year and Date
2009-04-20
Related Report
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