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A pH-gated conformational switch regulates the phosphatase activity of bifunctional HisKA-family histidine kinases

Author

Listed:
  • Yixiang Liu

    (Chinese Academy of Sciences)

  • Joshua Rose

    (Duke University Medical Center)

  • Shaojia Huang

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Yangbo Hu

    (Chinese Academy of Sciences)

  • Qiong Wu

    (Chinese Academy of Sciences)

  • Dan Wang

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Conggang Li

    (Chinese Academy of Sciences)

  • Maili Liu

    (Chinese Academy of Sciences)

  • Pei Zhou

    (Duke University Medical Center)

  • Ling Jiang

    (Chinese Academy of Sciences)

Abstract

Histidine kinases are key regulators in the bacterial two-component systems that mediate the cellular response to environmental changes. The vast majority of the sensor histidine kinases belong to the bifunctional HisKA family, displaying both kinase and phosphatase activities toward their substrates. The molecular mechanisms regulating the opposing activities of these enzymes are not well understood. Through a combined NMR and crystallographic study on the histidine kinase HK853 and its response regulator RR468 from Thermotoga maritima, here we report a pH-mediated conformational switch of HK853 that shuts off its phosphatase activity under acidic conditions. Such a pH-sensing mechanism is further demonstrated in the EnvZ-OmpR two-component system from Salmonella enterica in vitro and in vivo, which directly contributes to the bacterial infectivity. Our finding reveals a broadly conserved mechanism that regulates the phosphatase activity of the largest family of bifunctional histidine kinases in response to the change of environmental pH.

Suggested Citation

  • Yixiang Liu & Joshua Rose & Shaojia Huang & Yangbo Hu & Qiong Wu & Dan Wang & Conggang Li & Maili Liu & Pei Zhou & Ling Jiang, 2017. "A pH-gated conformational switch regulates the phosphatase activity of bifunctional HisKA-family histidine kinases," Nature Communications, Nature, vol. 8(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-02310-9
    DOI: 10.1038/s41467-017-02310-9
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