| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| 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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