Disaggregation mechanism of a ring shaped AAA+ chaperon
| Project/Area Number |
26440085
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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 |
Biophysics
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| Research Institution | Konan University |
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Principal Investigator |
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2016: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2015: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2014: ¥3,510,000 (Direct Cost: ¥2,700,000、Indirect Cost: ¥810,000)
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| Keywords | 分子シャペロン / 脱凝集 / ClpB / AAA+ / 協同性 / 凝集体 / AAA+タンパク質 / 分子シャペロンン |
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| Outline of Final Research Achievements |
ClpB is a ring shaped hexameric chaperone that can rescue heat-aggregated proteins. We prepared various ordered heterohexamers of ClpB, in which two subunits having different mutations were cross-linked to each other and arranged alternately. Using these heterohexamers, we cleared that each subunit of ClpB randomly binds ATP, and cooperatively hydrolyzes them.
Although DnaK chaperone cooperates with the ClpB, detailed analysis of this cooperation is difficult due to their low affinity. We constructed the DnaK-ClpB fusion protein and its mutants. By the analysis of these fusion proteins, we found that the DnaK can activate the ClpB ATPase activity only when the DnaK is in the closed form that can stably bind substrate proteins.
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Report
(4 results)
Research Products
(15 results)
