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Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases

Author

Listed:
  • Cristina Mideros-Mora

    (Consejo Superior de Investigaciones Científicas (IBV-CSIC)
    Facultad de Ciencias de la Salud Eugenio Espejo)

  • Laura Miguel-Romero

    (Consejo Superior de Investigaciones Científicas (IBV-CSIC)
    University of Glasgow)

  • Alonso Felipe-Ruiz

    (Consejo Superior de Investigaciones Científicas (IBV-CSIC))

  • Patricia Casino

    (Universitat de València
    Universitat de València
    CIBER de enfermedades raras (CIBERER-ISCIII))

  • Alberto Marina

    (Consejo Superior de Investigaciones Científicas (IBV-CSIC)
    CIBER de enfermedades raras (CIBERER-ISCIII))

Abstract

Histidine is a versatile residue playing key roles in enzyme catalysis thanks to the chemistry of its imidazole group that can serve as nucleophile, general acid or base depending on its protonation state. In bacteria, signal transduction relies on two-component systems (TCS) which comprise a sensor histidine kinase (HK) containing a phosphorylatable catalytic His with phosphotransfer and phosphatase activities over an effector response regulator. Recently, a pH-gated model has been postulated to regulate the phosphatase activity of HisKA HKs based on the pH-dependent rotamer switch of the phosphorylatable His. Here, we have revisited this model from a structural and functional perspective on HK853–RR468 and EnvZ–OmpR TCS, the prototypical HisKA HKs. We have found that the rotamer of His is not influenced by the environmental pH, ruling out a pH-gated model and confirming that the chemistry of the His is responsible for the decrease in the phosphatase activity at acidic pH.

Suggested Citation

  • Cristina Mideros-Mora & Laura Miguel-Romero & Alonso Felipe-Ruiz & Patricia Casino & Alberto Marina, 2020. "Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14540-5
    DOI: 10.1038/s41467-020-14540-5
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