コレラ菌走化性受容体ホモログの機能解析系の構築

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  • INDENTIFICATION OF NOVEL CHEMORECEPTORS IN VIBRIO CHOLERAE USING A NEWLY DEVELOPED FUNCTIONAL ASSAY SYSTEM

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Vibrio cholerae, the causative agent of cholera, shows chemotaxis to survive in various environments. The bacterium has 44 MCP-like proteins (MLPs) and three Che-related systems. This laboratory showed that Mlp24 and Mlp37 mediate attractant response to amino acids. However, other MLPs have been largely uncharacterized. A preliminary experiments suggest that the amino acid chemoreceptor Mlp24 can be coupled to CheA2 of V. cholerae in an Escherichia coli strain lacking all MCPs. If this is the case, the functions of V. cholerae MLPs can be employed in E. coli. Here I aimed at developing such a functional assay system. An E. coli strain lacking all MCPs as the histidine kinase CheA and the adaptor CheW was used to avoid undesirable cross-talk, if any, between V. cholerae MLP and E. coli CheA. Co-expression of Mlp24 with CheA2 and CheW1 of V. cholerae mediated responses to the repellent glycerol and the attractants arginine, glycine and serine. We then examined Mlp28 and Mlp29, and found that they also mediate repellent and attractant responses to these chemicals. However, Mlp28 and Mlp28 showed no methylation in the presence of these amino acids. Using this heterologous expression system, I also examined Che system III, the physiological significance of which is not known. E. coli cells co-expression Mlp45 with CheA3, CheW2 and CheW3 swarmed faster than control cells only under anaerobic conditions, a result consistent with the fact that anaerobic growth of V. cholerae cells induces polar localization of CheA3-GFP, raising the possibility that this signaling system functions under anaerobic conditions.

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