Proteolysis of histidine kinase VgrS inhibits its autophosphorylation and promotes osmostress resistance in Xanthomonas campestris

Chao-Ying Deng, Huan Zhang, Yao Wu, Li-Li Ding, Yue Pan, Shu-Tao Sun, Ya-Jun Li, Li Wang and Wei Qian ()
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Chao-Ying Deng: Chinese Academy of Sciences
Huan Zhang: Chinese Academy of Sciences
Yao Wu: Chinese Academy of Sciences
Li-Li Ding: Chinese Academy of Sciences
Yue Pan: Chinese Academy of Sciences
Shu-Tao Sun: Institute of Microbiology, Chinese Academy of Sciences
Ya-Jun Li: Chinese Academy of Sciences
Li Wang: Chinese Academy of Sciences
Wei Qian: Chinese Academy of Sciences

Nature Communications, 2018, vol. 9, issue 1, 1-15

Abstract: Abstract In bacterial cells, histidine kinases (HKs) are receptors that monitor environmental and intracellular stimuli. HKs and their cognate response regulators constitute two-component signalling systems (TCSs) that modulate cellular homeostasis through reversible protein phosphorylation. Here the authors show that the plant pathogen Xanthomonas campestris pv. campestris responds to osmostress conditions by regulating the activity of a HK (VgrS) via irreversible, proteolytic modification. This regulation is mediated by a periplasmic, PDZ-domain-containing protease (Prc) that cleaves the N-terminal sensor region of VgrS. Cleavage of VgrS inhibits its autokinase activity and regulates the ability of the cognate response regulator (VgrR) to bind promoters of downstream genes, thus promoting bacterial adaptation to osmostress.

Date: 2018
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DOI: 10.1038/s41467-018-07228-4

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