Phospho-mimetic CheV interacts with a subset of chemoreceptors

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...

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Autores: Matilla, Miguel A., Cano-Muñoz, Mario, Monteagudo-Cascales, Elizabet, Krell, Tino
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2025
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/413103
Acceso en línea:http://hdl.handle.net/10261/413103
Access Level:acceso abierto
Palabra clave:Chemotaxis
Chemoreceptor
Pseudomonas aeruginosa
CheV
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dc.title.none.fl_str_mv Phospho-mimetic CheV interacts with a subset of chemoreceptors
title Phospho-mimetic CheV interacts with a subset of chemoreceptors
spellingShingle Phospho-mimetic CheV interacts with a subset of chemoreceptors
Matilla, Miguel A.
Chemotaxis
Chemoreceptor
Pseudomonas aeruginosa
CheV
title_short Phospho-mimetic CheV interacts with a subset of chemoreceptors
title_full Phospho-mimetic CheV interacts with a subset of chemoreceptors
title_fullStr Phospho-mimetic CheV interacts with a subset of chemoreceptors
title_full_unstemmed Phospho-mimetic CheV interacts with a subset of chemoreceptors
title_sort Phospho-mimetic CheV interacts with a subset of chemoreceptors
dc.creator.none.fl_str_mv Matilla, Miguel A.
Cano-Muñoz, Mario
Monteagudo-Cascales, Elizabet
Krell, Tino
author Matilla, Miguel A.
author_facet Matilla, Miguel A.
Cano-Muñoz, Mario
Monteagudo-Cascales, Elizabet
Krell, Tino
author_role author
author2 Cano-Muñoz, Mario
Monteagudo-Cascales, Elizabet
Krell, Tino
author2_role author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia, Innovación y Universidades (España)
Agencia Estatal de Investigación (España)
Consejo Superior de Investigaciones Científicas (España)
Junta de Andalucía
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Chemotaxis
Chemoreceptor
Pseudomonas aeruginosa
CheV
topic Chemotaxis
Chemoreceptor
Pseudomonas aeruginosa
CheV
description 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.IMPORTANCECheV is one of the least understood chemosensory signaling proteins. Our demonstration that CheV interacts only with certain chemoreceptors offers fundamental new insights. These findings, combined with the observation that CheV is present in bacteria with numerous chemoreceptors, suggest that CheV plays a role in coordinating chemotactic outputs in complex chemosensory systems. Understanding the mechanisms by which chemotactic responses are defined in bacteria with a high number of chemoreceptors is a major research priority in the field of chemotaxis. While previous studies, including this one, show that the ability to be phosphorylated is crucial for CheV function, the molecular consequences of CheV phosphorylation have remained unclear. Our discovery that phosphorylation is essential for CheV binding to certain chemoreceptors fills in this critical gap in understanding the molecular mechanism of CheV. This study is likely to inspire further research into CheV function in other bacteria using similar approaches.
publishDate 2025
dc.date.none.fl_str_mv 2025
2026
2026
2026
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dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/413103
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dc.publisher.none.fl_str_mv American Society for Microbiology
publisher.none.fl_str_mv American Society for Microbiology
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
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spelling Phospho-mimetic CheV interacts with a subset of chemoreceptorsMatilla, Miguel A.Cano-Muñoz, MarioMonteagudo-Cascales, ElizabetKrell, TinoChemotaxisChemoreceptorPseudomonas aeruginosaCheVChemotaxis 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.IMPORTANCECheV is one of the least understood chemosensory signaling proteins. Our demonstration that CheV interacts only with certain chemoreceptors offers fundamental new insights. These findings, combined with the observation that CheV is present in bacteria with numerous chemoreceptors, suggest that CheV plays a role in coordinating chemotactic outputs in complex chemosensory systems. Understanding the mechanisms by which chemotactic responses are defined in bacteria with a high number of chemoreceptors is a major research priority in the field of chemotaxis. While previous studies, including this one, show that the ability to be phosphorylated is crucial for CheV function, the molecular consequences of CheV phosphorylation have remained unclear. Our discovery that phosphorylation is essential for CheV binding to certain chemoreceptors fills in this critical gap in understanding the molecular mechanism of CheV. This study is likely to inspire further research into CheV function in other bacteria using similar approaches.This study was supported by grants from the Spanish Ministry for Science, Innovation and Universities/Agencia Estatal de Investigación 10.13039/501100011033 (grants PID2020-112612GB-I00 and PID2023-146216NB-I00 to T.K. and PID2019- 103972GA-I00 and PID2023-146281NB-I00 to M.A.M.), the Consejo Superior de Investigaciones Científicas (grant 2024AEP062 to T.K.), and the Junta de Andalucía (grant P18-FR-1621 to T.K.). M.C.M. was supported by the post-doctoral training grant Juan de la Cierva JDC2022-049681-I.American Society for MicrobiologyMinisterio de Ciencia, Innovación y Universidades (España)Agencia Estatal de Investigación (España)Consejo Superior de Investigaciones Científicas (España)Junta de AndalucíaConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2026202620252026info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/413103reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2020-112612GB-I00info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2023-146216NB-I00info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-103972GA-I00info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2023-146281NB-I00http://dx.doi.org/10.1128/mbio.02874-25Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/4131032026-05-22T06:33:51Z
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