| Project/Area Number |
15380059
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Applied microbiology
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| Research Institution | Tokyo Institute of Technology |
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Principal Investigator |
WACHI Masaaki Tokyo Institute of Technology, Department of Bioscience and Biotechnology, Associate Professor, 大学院・生命理工学研究科, 助教授 (90192822)
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| Project Period (FY) |
2003 – 2005
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| Project Status |
Completed (Fiscal Year 2005)
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| Budget Amount *help |
¥14,500,000 (Direct Cost: ¥14,500,000)
Fiscal Year 2005: ¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 2004: ¥3,900,000 (Direct Cost: ¥3,900,000)
Fiscal Year 2003: ¥7,500,000 (Direct Cost: ¥7,500,000)
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| Keywords | RNase G / RNase E / Hfq / FtsZ / stress protection / RNA metabolism / adhE / アルコールデヒドロゲナーゼ / バリン / ピルビン酸 / 糖代謝 / Gad / 酸耐性 / エノラーゼ / cra / Dps / 酸化ストレス |
|---|
| Research Abstract |
In order to elucidate the regulatory mechanism of mRNA stability by the Escherichia coli endoribonuclease RNase G, action of RNase G on adhE mRNA was investigated. As a result, it was revealed that adhE mRNA cleaved by RNase G at -17 was rapidly degraded while one cleaved by RNase III at -31 was translated. It was found that RNase G mutant strains overproduced pyruvate because of increased stability of mRNAs encoding glycolysis enzymes. According to this finding, a new method for fermentative production of pyruvate and valine was established. It was found that processing of the ftsZ mRNA encoding the essential cell division protein FtsZ was an essential reaction of RNase E required for cell viability. In the RNase E mutant cells, translation of the unprocessed ftsZ mRNA was inhibited by the RNA-binding protein Hfq. For these results, it is suggested that mRNA stability control by endoribonucleases is widely involved in the regulatory mechanism of gene expression in E.coli.
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