| 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)
|
|---|
| 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.
|
