Structural studies on the cytosolic iron-sulfur cluster assembly (CIA) system
| Project/Area Number |
25440034
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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 |
Structural biochemistry
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| Research Institution | Ibaraki University (2015)
University of Hyogo (2013-2014) |
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Principal Investigator |
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2015: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2014: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2013: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
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| Keywords | 鉄硫黄クラスター / 金属タンパク質 / 分子シャペロン |
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| Outline of Final Research Achievements |
Iron-sulfur proteins assume a variety of roles in living cells and require systems for the assembly of iron-sulfur clusters. The iron-sulfur assembly (CIA) system has recently been identified as unique system for iron-sulfur cluster proteins in the eukaryotic cytosol and nucleus. We have started the structural studies on the components and complex of the CIA system in order to elucidate the exact pathway and reaction mechanisms. All the major components were successfully produced with E. coli expression systems after optimization of sequences, expression vectors, and hosts. The precursor of iron-sulfur clusters are unstable under aerobic condition, and therefore, they are purified and crystallized under anaerobic glove box. The Cia1 protein from C. elegans has been crystallized and the X-ray structure was determined to 1.5 angstrom resolution. The structure comparison revealed the local conformational divergence among species suggesting different protein interaction for each species.
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Report
(4 results)
Research Products
(2 results)
