2007 Fiscal Year Final Research Report Summary
The Voltage-Gated Na+ Channel Co-localizes with Methyl-Accepting Chemotaxis Proteins ofAlkaliphile at a Cell Pole
| Project/Area Number |
17613004
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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 |
極限環境生物学
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| Research Institution | Toyo University |
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Principal Investigator |
ITO Masahiro Toyo University, Department of Life Sciences, Associate Professor (80297738)
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| Project Period (FY) |
2005 – 2007
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| Keywords | Alkaliphiles / Chemotaxis / Na+ channel / Bacillus pseudofirmus / Extremopjhiles |
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| Research Abstract |
The bacterial ion channels are useful for the structural analysis of the eukaryotic ion channels. The elucidation of physiologic functions and effecter proteins of the bacterial ion channels is important in research of the ion channels. NavBP is the member of the bacterial voltage-gated Na+ channel superfamily that is found in alkaliphilic Bacillus pseudofirmus OF4. NavBP has recently been shown to have a role in pH homeostasis, motility and chemotaxis. The chemotaxis phenotype of NavBP deletion mutant was particularly striking in that the response of the mutants to chemoattractants was inverted compared to the wild-type strain. Therefore, we have studied to elucidate the relation of the deficit of Na channel and the abnormalities in chemotaxis. We have already reported the following things. First, in the wild-type strain, colocalization of NavBP and the putative chemotaxis receptor McpX was observed at cell pole by immuno fluorescent microscopy (IFM). Second, in the NavBP deletion mutant, although the expression level of McpX did not change mostly, but the localization of that was decreased. Then, in order to observe cellullar localization of NavBP in a live cell, the plasmid which express the NavBP-CFP fusion protein was constructed, the transformation was carried out to NavBP deletion mutant. As a result, polar localization of functional NavBP-CFP was observed. The polar localization of NavBP in alkaliphilic Bacillus pseudofirmus OF4 was strongly suggested. In order for a chemotaxis receptor to function, it is necessary to localized at cell pole. The results suggest interactions between NavBP and McpX that affect their co-localization at cell pole. The inverse chemotaxis phenotype of NavBP deletion mutants may result in part from delocalization of McpX.
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[Presentation] The voltage-gated Na+ channel NavBP co-localizes with methyl-accepting chemotaxis protein at cell poles of alkaliphilic Bacillus pseudofirmus OF42008
Author(s)
Ito, M, Fujinami, S., Sato, T., Kawagishi, I., Krulwich, T.A.
Organizer
Gordon Research Conferences "SENSORY TRANSDUCTION IN MICROORGANISMS
Place of Presentation
Ventura, CA, USA
Year and Date
20080113-18
Description
「研究成果報告書概要(欧文)」より
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[Presentation] The Voltage- Gated Na+ Channel NavBP Co-localizes with Methyl-Accepting Chemotaxis Protein at Cell Poles of Alkaliphilic Bacillus pseudofirmus OF42008
Author(s)
Ito, M, Fujinami, S., Sato, T.,Krulwich, T.A., Kawagishi, I.
Organizer
2008 General meeting of Japan Society for Bioscience, Biotechnology, and Agrochemistry
Place of Presentation
Nagoya
Year and Date
2008-03-28
Description
「研究成果報告書概要(欧文)」より
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[Presentation] The visualization of the voltage-gated Na+ channel of Alkaliphilic Bacillus pseudofirmus OF4 by using fluorescent protein fusion2007
Author(s)
Fujinami, S, Sato, T., Krulwich, T.A., Kawagishi, I., Ito, M.
Organizer
1st Kanto brunch meeting of Japanese society for Bioscience, Biotechnology, and, Agrochemistry
Place of Presentation
Utsunomiya
Year and Date
2007-11-10
Description
「研究成果報告書概要(欧文)」より
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[Book] Physiology and Biochemistry of Extremophiles(Gerday, C.and Glansdorff, N., eds.)2006
Author(s)
Krulwich, T.A., Hicks, D.B., Swartz, T.H., Ito, M.
Total Pages
429
Publisher
ASM Press(アメリカ微生物学会出版),Washington,DC.
Description
「研究成果報告書概要(和文)」より
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