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

Yixiang Liu, Joshua Rose, Shaojia Huang, Yangbo Hu, Qiong Wu, Dan Wang, Conggang Li, Maili Liu, Pei Zhou and Ling Jiang ()
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Yixiang Liu: Chinese Academy of Sciences
Joshua Rose: Duke University Medical Center
Shaojia Huang: Chinese Academy of Sciences
Yangbo Hu: Chinese Academy of Sciences
Qiong Wu: Chinese Academy of Sciences
Dan Wang: 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

Nature Communications, 2017, vol. 8, issue 1, 1-10

Abstract: 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.

Date: 2017
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DOI: 10.1038/s41467-017-02310-9

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