2017 Fiscal Year Final Research Report
The elucidation of the folding acceleration mechanism of prokaryotic and eukaryotic chaperonins
| Project/Area Number |
15K06983
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | Toyama Prefectural University |
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Principal Investigator |
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Keywords | 分子シャペロン / 変性 / フォールディング |
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| Outline of Final Research Achievements |
We tested whether denatured protein encapsulated in the chaperonin cage is expanded by using single-pair FRET. All of tested substrate proteins were more expanded in the chaperonin cage than those at the initial of spontaneous folding. Mutational analysis revealed that hydrophobic residues in the chaperonin cage differently reduced the folding acceleration ability and the inhibition of polypeptide escape. To elucidate whether the folding acceleration mechanism can be applied to eukaryotic chaperonin CCT, we constructed the recombinant expression system of CCT from Cyanidioschyzon merolae. The recombinant CCT bounds fluorescent ATP analog, Cy3-ATP. The crystallization condition of CCT was searched in the presence of various nucleotide analogs. However, we could not obtain the crystal of CCT.
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| Free Research Field |
生化学、構造生物物理学
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