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Phosphorylated CheV interacts with a subset of chemoreceptors
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Phosphorylated CheV interacts with a subset of chemoreceptors
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Paper
Phosphorylated CheV interacts with a subset of chemoreceptors
2025
Overview
Chemotaxis pathways are among the most complex signaling systems in bacteria. A central feature of these pathways is the ternary complex formed by chemoreceptors, the autokinase CheA, and the coupling proteins CheW and CheV. Whereas CheW is present in all chemotaxis pathways, CheV is primarily found in bacteria that contain many chemoreceptors. CheV is a fusion of a CheW-like domain to a phosphorylatable receiver domain. The roles of CheV and its phosphorylation are currently uncertain. Pseudomonas aeruginosa contains many chemoreceptors for which the cognate signals have been identified. Quantitative capillary chemotaxis assays of a cheV mutant revealed that responses to certain chemoeffectors, such as nitrate and α-ketoglutarate, were drastically reduced, while responses to others, such as amino acids and inorganic phosphate, were comparable to the wild type, indicating that CheV selectively acts on specific chemoreceptors. To study the mechanism of CheV action, we conducted protein-protein interaction experiments using isothermal titration calorimetry. These studies showed that unphosphorylated CheV fails to bind to cytosolic fragments of the McpN and PctA chemoreceptors, which mediate responses to nitrate and amino acids, respectively. In contrast, the phosphorylation-mimic CheV D238E bound with very high affinity (KD = 8 nM) to McpN but failed to interact with PctA. Thus, CheV in P. aeruginosa binds to some chemoreceptors but not to others in a phosphorylation-dependent manner. These results suggest that CheV is a regulatory protein that modulates signaling through specific chemoreceptors. CheV may thus facilitate the coordination of chemotaxis responses in complex, multi-chemoreceptor systems.
Publisher
Cold Spring Harbor Laboratory Press,Cold Spring Harbor Laboratory
