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An NLR paralog Pit2 generated from tandem duplication of Pit1 fine-tunes Pit1 localization and function

Author

Listed:
  • Yuying Li

    (Chinese Academy of Agricultural Sciences
    Chinese Academy of Sciences)

  • Qiong Wang

    (Chinese Academy of Sciences
    Yangzhou University)

  • Huimin Jia

    (Jiangxi Agricultural University)

  • Kazuya Ishikawa

    (Chinese Academy of Sciences
    Ritsumeikan University)

  • Ken-ichi Kosami

    (Chinese Academy of Sciences
    Ehime Research Institute of Agriculture, Forestry and Fisheries)

  • Takahiro Ueba

    (Nara Institute of Science and Technology)

  • Atsumi Tsujimoto

    (Nara Institute of Science and Technology)

  • Miki Yamanaka

    (Nara Institute of Science and Technology)

  • Yasuyuki Yabumoto

    (Nara Institute of Science and Technology)

  • Daisuke Miki

    (Chinese Academy of Sciences)

  • Eriko Sasaki

    (Kyushu University)

  • Yoichiro Fukao

    (Ritsumeikan University)

  • Masayuki Fujiwara

    (Ltd.)

  • Takako Kaneko-Kawano

    (Ritsumeikan University)

  • Li Tan

    (Chinese Academy of Sciences)

  • Chojiro Kojima

    (Yokohama National University)

  • Rod A. Wing

    (University of Arizona)

  • Alfino Sebastian

    (Okayama University)

  • Hideki Nishimura

    (Okayama University)

  • Fumi Fukada

    (Okayama University)

  • Qingfeng Niu

    (Anhui Agricultural University, Research Centre for Biological Breeding Technology)

  • Motoki Shimizu

    (Iwate Biotechnology Research Center)

  • Kentaro Yoshida

    (Kyoto University)

  • Ryohei Terauchi

    (Iwate Biotechnology Research Center
    Kyoto University)

  • Ko Shimamoto

    (Nara Institute of Science and Technology)

  • Yoji Kawano

    (Chinese Academy of Sciences
    Okayama University
    Yokohama City University)

Abstract

NLR family proteins act as intracellular receptors. Gene duplication amplifies the number of NLR genes, and subsequent mutations occasionally provide modifications to the second gene that benefits immunity. However, evolutionary processes after gene duplication and functional relationships between duplicated NLRs remain largely unclear. Here, we report that the rice NLR protein Pit1 is associated with its paralogue Pit2. The two are required for the resistance to rice blast fungus but have different functions: Pit1 induces cell death, while Pit2 competitively suppresses Pit1-mediated cell death. During evolution, the suppression of Pit1 by Pit2 was probably generated through positive selection on two fate-determining residues in the NB-ARC domain of Pit2, which account for functional differences between Pit1 and Pit2. Consequently, Pit2 lost its plasma membrane localization but acquired a new function to interfere with Pit1 in the cytosol. These findings illuminate the evolutionary trajectory of tandemly duplicated NLR genes after gene duplication.

Suggested Citation

  • Yuying Li & Qiong Wang & Huimin Jia & Kazuya Ishikawa & Ken-ichi Kosami & Takahiro Ueba & Atsumi Tsujimoto & Miki Yamanaka & Yasuyuki Yabumoto & Daisuke Miki & Eriko Sasaki & Yoichiro Fukao & Masayuki, 2024. "An NLR paralog Pit2 generated from tandem duplication of Pit1 fine-tunes Pit1 localization and function," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
  • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-48943-5
    DOI: 10.1038/s41467-024-48943-5
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    References listed on IDEAS

    as
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