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

Author

Listed:
  • Chao-Ying Deng

    (Chinese Academy of Sciences)

  • Huan Zhang

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

  • Yao Wu

    (Chinese Academy of Sciences)

  • Li-Li Ding

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

  • Yue Pan

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

  • Shu-Tao Sun

    (Institute of Microbiology, Chinese Academy of Sciences)

  • Ya-Jun Li

    (Chinese Academy of Sciences
    Beijing Forestry University)

  • Li Wang

    (Chinese Academy of Sciences)

  • Wei Qian

    (Chinese Academy of Sciences)

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.

Suggested Citation

  • Chao-Ying Deng & Huan Zhang & Yao Wu & Li-Li Ding & Yue Pan & Shu-Tao Sun & Ya-Jun Li & Li Wang & Wei Qian, 2018. "Proteolysis of histidine kinase VgrS inhibits its autophosphorylation and promotes osmostress resistance in Xanthomonas campestris," Nature Communications, Nature, vol. 9(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07228-4
    DOI: 10.1038/s41467-018-07228-4
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