N-terminal domain including conserved flg22 is required for flagellin-induced hypersensitive cell death in Arabidopsis thaliana

  • NAITO Kana
    Laboratory of Plant Pathology and Genetic Engineering, Graduate School of Natural Science and Technology, Okayama University
  • ISHIGA Yasuhiro
    Laboratory of Plant Pathology and Genetic Engineering, Graduate School of Natural Science and Technology, Okayama University
  • TOYODA Kazuhiro
    Laboratory of Plant Pathology and Genetic Engineering, Graduate School of Natural Science and Technology, Okayama University
  • SHIRAISHI Tomonori
    Laboratory of Plant Pathology and Genetic Engineering, Graduate School of Natural Science and Technology, Okayama University
  • ICHINOSE Yuki
    Laboratory of Plant Pathology and Genetic Engineering, Graduate School of Natural Science and Technology, Okayama University

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<p>Flagellin in Pseudomonas syringae is a potent elicitor of defense responses including hypersensitive cell death in dicot plants. The oligopeptides flg22 consisting of 22 conserved amino acids near the N-terminus of flagellins is reported to induce plant defense responses. Because glycosylation of the central domain of flagellin affects its elicitor activity, we investigated whether any peptide sequence in addition to flg22 is required for flagellin-induced hypersensitive reaction. A study of recombinant flagellin polypeptides indicated that the N-terminal domain including the conserved flg22 is required for flagellin-induced hypersensitive cell death in Arabidopsis thaliana.</p>

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