The Voltage-Gated Na+ Channel Co-localizes with Methyl-Accepting Chemotaxis Proteins ofAlkaliphile at a Cell Pole

电压门控Na通道与细胞极上嗜碱菌的甲基接受趋化蛋白共定位

基本信息

批准号：
17613004
负责人：
ITO Masahiro
金额：
$ 2.43万
依托单位：
Toyo University
依托单位国家：
日本
项目类别：
Grant-in-Aid for Scientific Research (C)
财政年份：
2005
资助国家：
日本
起止时间：
2005 至 2007
项目状态：
已结题

来源：
https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-17613004/
关键词：
Alkaliphiles Chemotaxis Na+ channel Bacillus pseudofirmus Extremopjhiles ナトリウムチャネル

项目摘要

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.

细菌离子通道可用于真核离子通道的结构分析。细菌离子通道的生理功能和效应蛋白的阐明在离子通道的研究中很重要。 NAVBP是细菌电压门控的Na+通道超家族的成员，该通道在4的碱性芽孢杆菌中发现。最近已显示NAVBP在pH稳态，运动性和趋化性中起作用。 NAVBP缺失突变体的趋化性表型尤其引人注目，因为与野生型菌株相比，突变体对化学吸引剂的响应被反倒。因此，我们研究了阐明Na通道不足和趋化性异常的关系。我们已经报告了以下内容。首先，在野生型菌株中，通过免疫荧光显微镜（IFM）观察到NAVBP的共定位和假定的趋化受体MCPX。其次，在NAVBP缺失突变体中，尽管MCPX的表达水平并没有大大变化，但其定位却降低了。然后，为了观察NAVBP在活细胞中的手机定位，构建了NAVBP-CFP融合蛋白的质粒，进行了转换，以进行NAVBP缺失突变体。结果，观察到功能性NAVBP-CFP的极性定位。强烈建议NAVBP在碱性杆菌中的极性定位。为了使趋化受体起作用，必须定位在细胞极。结果表明，NAVBP和MCPX之间的相互作用会影响其在细胞极点的共定位。 NAVBP缺失突变体的趋化趋化表型可能会导致MCPX的离域化。

项目成果

期刊论文数量（0）

专著数量（0）

科研奖励数量（0）

会议论文数量（0）

专利数量（0）

The Vbltage-Gated Na^+ Channel Na_vBP Co-localizes with Methyl-Accepting Chemotaxis Protein at Cell Poles of Alkaliphilic Bacillus pseudofrrmus OF4

Vbltage-门控Na^通道Na_vBP与嗜碱芽孢杆菌OF4细胞极的甲基接受趋化蛋白共定位

DOI：
发表时间：
2007
期刊：
Microbiology誌 153(12)
影响因子：
0
作者：
Fujinami S.;T. Sato;J.S. Trimmer;B.W. Spillcr;D.E. Clapham;T.A. Krulwich;I. Kawagishi;M. Ito
通讯作者：
M. Ito

生体におけるナトリウムイオンサイクル:好アルカリ性バチルス属細菌で見つかった2つのナトリウムチャネル

活生物体中的钠离子循环：嗜碱芽孢杆菌中发现的两个钠通道