| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2017: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2016: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2015: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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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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