Mechanism of regulation of E. coli cell duplication by DNA-, RNA- binding protein Hfq
| Project/Area Number |
12660069
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
応用微生物学・応用生物化学
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| Research Institution | Tokyo Institute of Technology |
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Principal Investigator |
WACHI Masaaki Tokyo Inst. Technol., Dept. Bioengineering, Associate Professor, 大学院・生命理工学研究科, 助教授 (90192822)
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| Project Period (FY) |
2000 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥4,100,000 (Direct Cost: ¥4,100,000)
Fiscal Year 2001: ¥1,700,000 (Direct Cost: ¥1,700,000)
Fiscal Year 2000: ¥2,400,000 (Direct Cost: ¥2,400,000)
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| Keywords | iron ion / oxidative stress / Hfq / RNaseE / RNase G / mRNA / rRNA / 大腸菌 / 細胞増殖 / Hfqタンパク質 / DNA損傷 |
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| Research Abstract |
FepA and FhuE proteins involved in iron transport in the outer-membrane were overproduced in the hfq::cat mutant cells. The hfq::cat mutant was more susceptible to killing by hydrogen peroxide, probably due to the excess incorporation of iron. Direct measurement of intracellular iron concentrations by electroparamagnetic resonance spectroscopy revealed that the mutant cells indeed accumulated significantly higher levels of iron than the wild type cells. The Hfq protein protected DNA from iron-induced oxidative damages in vitro. These results suggest that the Hfq protein is involved in the mechanism of cell survival by protecting cells from oxidative stress.
Genetic interaction between hfq and RNazes was examined. Temperature sensitivity of the ams-1 (RNaze E^<ts>) mutant strain was suppressed by introduction of the hfq::cat mutation. Its suppression was cancelled by introduction of mg::cat (RNaze G defective) mutation. These results suggest that the Hfq protein is involved in the mechanism of regulation of mRNA stability by RNaze E and RNaze G.
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Report
(3 results)
Research Products
(26 results)
