2012 Fiscal Year Final Research Report
Functional and kinetic analysis of the inter-domain communication network of the chaperonin GroEL
| Project/Area Number |
22570119
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | Tottori University |
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Principal Investigator |
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| Project Period (FY) |
2010 – 2012
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| Keywords | 変性とフォールディング / シャペロニン / ストップト・フロー解析 / 円順列変異 |
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| Research Abstract |
A combination of circular permutation and stopped-flow fluorescence analysis was utilized to probe the relationship between the molecular mechanism of GroEL-facilitated protein folding and the unique three-domain subunit structure of the GroEL protein. Through analysis of multiple circularly permuted GroEL variants, we succeeded in correlating a specific, domain-dependent conformational change to an important functional aspect of the chaperonin mechanism. Additionally, our results prompt a reevaluation of the conventional mechanism of GroEL-facilitated folding.
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