Studies on the subunit cooperative mechanism in the reaction cycle of group 2 chaperonin
| Project/Area Number |
24370064
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | Tokyo University of Agriculture and Technology |
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Principal Investigator |
YOHDA MASAFUMI 東京農工大学, 工学(系)研究科(研究院), 教授 (50250105)
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| Co-Investigator(Kenkyū-buntansha) |
SEKIGUCHI Hiroshi 公益財団法人高輝度光科学研究センター, 利用研究促進部門, 研究員 (00401563)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥18,330,000 (Direct Cost: ¥14,100,000、Indirect Cost: ¥4,230,000)
Fiscal Year 2014: ¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2013: ¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2012: ¥7,800,000 (Direct Cost: ¥6,000,000、Indirect Cost: ¥1,800,000)
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| Keywords | フォールディング / シャペロン / 構造変化機構 / 古細菌 / シャペロニン / 構造変化 |
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| Outline of Final Research Achievements |
Group 2 chaperonin (CPN) plays important roles in proteostasis in cytosol of eukaryotes or archaea. The aim of this study is to reveal the detailed protein folding mechanism of CPN. By kinetic analyses using stopped-flow fluorometry and diffracted X-ray tracking, we could dissect the conformational change process of CPN. ATP binding to each subunit causes conformational change and cooperation of subunits in the ring induces transition from open to closed conformation. Then, the ring twisted counterclockwise in ATP hydrolysis manner to induce folding of the protein in the cavity. Subsequently, the ring reverts to the original state by a clockwise twist to release the folded protein. Finally, we have succeeded to construct asymmetric CPN, CPN-ASP, in which one ring is composed of wild type subunits and the other one of mutant subunits. By charactering CPN-ASP, we have shown that the inter-ring communication is dispensable in the reaction cycle of CPN.
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Report
(4 results)
Research Products
(54 results)
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[Journal Article] Dissection of the ATP-dependent conformational change cycle of a group II chaperonin.2014
Author(s)
Nakagawa A, Moriya K, Arita M, Yamamoto Y, Kitamura K, Ishiguro N, Kanzaki T, Oka T, Makabe K, Kuwajima K, Yohda M.
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Journal Title
J Mol Biol.
Volume: 426
Issue: 2
Pages: 447-459
DOI
Related Report
Peer Reviewed
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[Journal Article] Expression, purification, crystallization and preliminary crystallographic analysis of hepatitis B virus core protein dimerized via a peptide linker containing an EGFP insertion2013
Author(s)
M.Kikuchi, S.Iwabuchi, T.Kikkou, K.Noguchi, M.Odaka, M.Yohda, M.Kawata, C.Sato, O.Matsumoto
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Journal Title
Acta Cryst
Volume: F69
Issue: 8
Pages: 942-945
DOI
Related Report
Peer Reviewed
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[Journal Article] ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking.2013
Author(s)
Sekiguchi H, Nakagawa A, Moriya K, Makabe K, Ichiyanagi K, Nozawa S, Sato T, Adachi S, Kuwajima K, Yohda M, Sasaki YC.
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Journal Title
PLoS One
Volume: 8
Issue: 5
Pages: e64176-e64176
DOI
Related Report
Peer Reviewed
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[Journal Article] Two arginine residues in the substrate pocket predominantly control the substrate selectivity of thiocyanate hydrolase2013
Author(s)
Yasuaki Yamanaka, Takatoshi Arakawa, Toshinori Watanabe, Satoshi Namima, Masa Sato, Shota Hori, Akashi Ohtaki, Keiichi Noguchi, Yoko Katayama, Masafumi Yohda, Masafumi Odaka
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Journal Title
Journal of Bioscience and Bioengineering
Volume: Vol. 116、Issue 1
Issue: 1
Pages: 22-27
DOI
NAID
Related Report
Peer Reviewed
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[Presentation] X線1分子追跡法による11型シャペロニン協同性評価2012
Author(s)
Hiroshi Sekiguchi, Ayumi Nakagawa, Kazuki Moriya, Mayuno Arita, Yohei Yamamoto, Kohei Ichiyanagi, Masafumi Yohda, Naoto Yagi, Yuji Sakaki
Organizer
日本生物物理学会第50回年会
Place of Presentation
名古屋大学東山キャンパス
Year and Date
2012-09-23
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