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<p>Chemotaxis is an adaptive mechanism that shapes the behavior of motile bacteria in habitats characterized by fluctuating and often conflicting cues environmental (e.g. stay-or-go). Chemotactic responses are orchestrated by phosphorylation of CheY, which triggers rotational switching of the flagella. In <i>Escherichia coli</i> and similar taxa, CheZ is the principal CheY-P phosphatase, whereas in lineages lacking CheZ, members of the structurally distinct CheC-FliY-CheX family fulfill this role. Intriguingly, some bacteria code for CheX and CheZ, presenting a conundrum regarding their function, and the role of CheX in CheZ-containing organisms is unknown. We imposed a sustained motility constraint under conditions of looming nutrient depletion in <i>Vibrio vulnificus</i>, which possesses both CheX and CheZ, using the c-di-GMP effector PlzD that robustly curtails swimming motility. Our analyses revealed that the activity of CheX, but not CheZ, could be attenuated to mitigate the imposed constraint, assigning CheX a pivotal function in fine-tuning foraging behavior during a “stay-or-go” decision. <i>V. vulnificus</i> CheX maintained CheY-P phosphatase activity despite its conserved dimeric fold structure exhibiting divergence in active-site architecture, suggesting a preserved catalytic mechanism among distantly related homologs. Co-conservation of <i>cheX</i> and <i>cheZ</i> across disparate bacterial phyla suggests their adaptative retention confers robustness and versatility to chemotactic control.</p>

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Altering chemotaxis as a strategy to enhance the foraging range of motility-restricted bacteria

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年1月6日

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  • Abigael Frederick,
  • Carolina Lopes,
  • Ben Fulton,
  • Yuhsun Huang,
  • Ram Podicheti,
  • Douglas Rusch,
  • George Minasov,
  • Ludmilla Shuvalova,
  • Karla J. F. Satchell,
  • Dean A. Rowe-Magnus

摘要

Chemotaxis is an adaptive mechanism that shapes the behavior of motile bacteria in habitats characterized by fluctuating and often conflicting cues environmental (e.g. stay-or-go). Chemotactic responses are orchestrated by phosphorylation of CheY, which triggers rotational switching of the flagella. In Escherichia coli and similar taxa, CheZ is the principal CheY-P phosphatase, whereas in lineages lacking CheZ, members of the structurally distinct CheC-FliY-CheX family fulfill this role. Intriguingly, some bacteria code for CheX and CheZ, presenting a conundrum regarding their function, and the role of CheX in CheZ-containing organisms is unknown. We imposed a sustained motility constraint under conditions of looming nutrient depletion in Vibrio vulnificus, which possesses both CheX and CheZ, using the c-di-GMP effector PlzD that robustly curtails swimming motility. Our analyses revealed that the activity of CheX, but not CheZ, could be attenuated to mitigate the imposed constraint, assigning CheX a pivotal function in fine-tuning foraging behavior during a “stay-or-go” decision. V. vulnificus CheX maintained CheY-P phosphatase activity despite its conserved dimeric fold structure exhibiting divergence in active-site architecture, suggesting a preserved catalytic mechanism among distantly related homologs. Co-conservation of cheX and cheZ across disparate bacterial phyla suggests their adaptative retention confers robustness and versatility to chemotactic control.