2015 Fiscal Year Final Research Report
Re-evaluation of the molecular mechanism of chaperonin action: characterization of circularly-permuted GroEL
Project/Area Number |
25440026
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Structural biochemistry
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Research Institution | Tottori University |
Principal Investigator |
Mizobata Tomohiro 鳥取大学, 工学(系)研究科(研究院), 准教授 (50263489)
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Project Period (FY) |
2013-04-01 – 2016-03-31
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Keywords | シャペロニン / ストップト・フロー解析 / 円順列変異 / フォールディング |
Outline of Final Research Achievements |
Chaperonins facilitate the folding of numerous proteins by binding to aggregation-prone protein molecules and isolating them from solution. During this process, chaperonins typically alter their subunit conformations dynamically in response to ATP binding and hydrolysis. To understand this mechanism at the molecular level, in this study we analyzed and compared functionally impaired mutant versions of the bacterial chaperonin GroEL using stopped-flow fluorescence analysis. Our results showed that numerous molecular events, such as the expansion of the molecular capsule that segregates denatured protein and the binding of co-chaperonins that form the lid of the "capsule", occur simultaneously upon completion of a specific conformational transition in GroEL. We also determined that specific conformational changes alter the affinity of GroEL toward denatured proteins, and this allows a smooth transition of the molecular mechanism through multiple cycles.
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Free Research Field |
細胞内外蛋白質フォールディングの物理化学的解析
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