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Cryptic bioactivity capacitated by synthetic hybrid plant peptides

Author

Listed:
  • Yuki Hirakawa

    (Institute of Transformative Bio-Molecules (WPI-ITbM), Nagoya University, Furo-cho)

  • Hidefumi Shinohara

    (Graduate School of Science, Nagoya University)

  • Kai Welke

    (Institute of Transformative Bio-Molecules (WPI-ITbM), Nagoya University, Furo-cho
    Graduate School of Science, Nagoya University)

  • Stephan Irle

    (Institute of Transformative Bio-Molecules (WPI-ITbM), Nagoya University, Furo-cho
    Graduate School of Science, Nagoya University)

  • Yoshikatsu Matsubayashi

    (Graduate School of Science, Nagoya University)

  • Keiko U. Torii

    (Institute of Transformative Bio-Molecules (WPI-ITbM), Nagoya University, Furo-cho
    Graduate School of Science, Nagoya University
    University of Washington
    Howard Hughes Medical Institute, University of Washington)

  • Naoyuki Uchida

    (Institute of Transformative Bio-Molecules (WPI-ITbM), Nagoya University, Furo-cho
    Graduate School of Science, Nagoya University)

Abstract

Evolution often diversifies a peptide hormone family into multiple subfamilies, which exert distinct activities by exclusive interaction with specific receptors. Here we show that systematic swapping of pre-existing variation in a subfamily of plant CLE peptide hormones leads to a synthetic bifunctional peptide that exerts activities beyond the original subfamily by interacting with multiple receptors. This approach provides new insights into the complexity and specificity of peptide signalling.

Suggested Citation

  • Yuki Hirakawa & Hidefumi Shinohara & Kai Welke & Stephan Irle & Yoshikatsu Matsubayashi & Keiko U. Torii & Naoyuki Uchida, 2017. "Cryptic bioactivity capacitated by synthetic hybrid plant peptides," Nature Communications, Nature, vol. 8(1), pages 1-7, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14318
    DOI: 10.1038/ncomms14318
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