期刊
MOLECULAR MICROBIOLOGY
卷 95, 期 5, 页码 780-790出版社
WILEY-BLACKWELL
DOI: 10.1111/mmi.12887
关键词
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资金
- Japan Society for Promotion of Science (JSPS)
- Ministry of Education, Culture, Sports, Science and Technology of Japan (MEXT)
- MEXT
- Grants-in-Aid for Scientific Research [24117004, 24657108, 23247024, 25000013] Funding Source: KAKEN
Vibrio cholerae has three sets of chemotaxis-related signaling proteins, of which only System II has been shown to be involved in chemotaxis. Here, we examined localization of green fluorescent protein (GFP)-fused components of System I. The histidine kinase (CheA1) and the adaptor (CheW0) of System I localized to polar and lateral membrane regions with standing incubation (microaerobic conditions), but their localization was lost after shaking (aerobic conditions). A transmembrane receptor of System I also showed polar and lateral localization with standing incubation. By contrast, GFP-fused components of System II localized constitutively to the flagellated pole. Nitrogen gas, sodium azide or carbonylcyanide m-chlorophenylhydrazone induced localization of CheA1-GFP even with shaking incubation, suggesting that the localization is controlled in response to changes in energy metabolism. Fluorescently labeled tetracysteine-tagged CheA1 also showed azide-induced localization, arguing against artifactual effects of GFP fusions. These results suggest that System I components are assembled into the supramolecular signaling complex in response to reduced cellular energy states, raising the possibility that the System I complex plays a role in sensing and signaling under microaerobic environments, such as in the host intestine.
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