2011 Fiscal Year Final Research Report
Structural change and function of ClpB chaperone disaggregase
| Project/Area Number |
21770151
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Functional biochemistry
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| Research Institution | Konan University |
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Principal Investigator |
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| Project Period (FY) |
2009 – 2011
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| Keywords | 酵素の触媒機構 |
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| Research Abstract |
ClpB can rescue the aggregated proteins(disaggregation). When the motion of N domain was restricted by the disulfide bond, the disaggregation activity of ClpB reduced. We found that the cause is in the threading-through process following the substrate-binding process. Moreover, we made two ClpB mutants in which two or six adjacent subunits of ClpB hexamer were cross-linked by the disulfide bond(s). Using these mutants, we found that the efficient disaggregation by ClpB required the moderate dissociation/association of the hexamer.
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