Molecular mechanism of the supramolecular machinery involved in biosynthesis of labile iron-sulfur clusters
| Project/Area Number |
24570148
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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 |
Functional biochemistry
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| Research Institution | Saitama University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
FUKUYAMA Keiichi 大阪大学, 工学(系)研究科, 招聘研究員 (80032283)
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| Project Period (FY) |
2012-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2013: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2012: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | 鉄硫黄タンパク質 / 鉄硫黄クラスター / 生合成 / マシナリー / 分子生物学 |
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| Outline of Final Research Achievements |
Biological assembly of iron-sulfur (Fe-S) clusters is mediated by complex systems consisting of multiple proteins. In this study, we have characterized two distinct systems called the ISC and SUF machineries in Escherichia coli. We found that modification of the isoprenoid biosynthetic pathway in E. coli can offset the indispensability of the Fe-S cluster biosynthetic systems and show that the resulting Δisc Δsuf double mutants can grow without detectable Fe-S cluster cluster containing proteins. We constructed and characterized a series of mutants and found hitherto unrecognized roles of some ISC components. We also determined the first crystal structure of the E. coli SufBCD complex that functions in the SUF machinery as a scaffold for the de novo Fe-S cluster assembly.
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Report
(5 results)
Research Products
(46 results)
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[Journal Article] Functional Dynamics Revealed by the Structure of the SufBCD Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as a Scaffold for Iron-Sulfur Cluster Biogenesis.2015
Author(s)
Hirabayashi K, Yuda E, Tanaka N, Katayama S, Iwasaki K, Matsumoto T, Kurisu G, Outten FW, Fukuyama K, Takahashi Y, Wada K.
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Journal Title
Journal of Biological Chemistry
Volume: 290
Issue: 50
Pages: 29717-29731
DOI
Related Report
Peer Reviewed / Int'l Joint Research
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