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An E2-E3 pair contributes to seed size control in grain crops

Author

Listed:
  • Sha Tang

    (Chinese Academy of Agricultural Sciences)

  • Zhiying Zhao

    (Chinese Academy of Agricultural Sciences)

  • Xiaotong Liu

    (Hebei Normal University
    Chinese Academy of Sciences)

  • Yi Sui

    (Chinese Academy of Agricultural Sciences)

  • Dandan Zhang

    (Chinese Academy of Agricultural Sciences)

  • Hui Zhi

    (Chinese Academy of Agricultural Sciences)

  • Yuanzhu Gao

    (Chinese Academy of Agricultural Sciences)

  • Hui Zhang

    (Chinese Academy of Agricultural Sciences)

  • Linlin Zhang

    (China Agricultural University)

  • Yannan Wang

    (Chinese Academy of Agricultural Sciences)

  • Meicheng Zhao

    (Chinese Academy of Sciences)

  • Dongdong Li

    (China Agricultural University)

  • Ke Wang

    (Chinese Academy of Agricultural Sciences)

  • Qiang He

    (Chinese Academy of Agricultural Sciences)

  • Renliang Zhang

    (Chinese Academy of Agricultural Sciences)

  • Wei Zhang

    (Chinese Academy of Agricultural Sciences)

  • Guanqing Jia

    (Chinese Academy of Agricultural Sciences)

  • Wenqiang Tang

    (Hebei Normal University)

  • Xingguo Ye

    (Chinese Academy of Agricultural Sciences)

  • Chuanyin Wu

    (Chinese Academy of Agricultural Sciences)

  • Xianmin Diao

    (Chinese Academy of Agricultural Sciences)

Abstract

Understanding the molecular mechanisms that regulate grain yield is important for improving agricultural productivity. Protein ubiquitination controls various aspects of plant growth but lacks understanding on how E2-E3 enzyme pairs impact grain yield in major crops. Here, we identified a RING-type E3 ligase SGD1 and its E2 partner SiUBC32 responsible for grain yield control in Setaria italica. The conserved role of SGD1 was observed in wheat, maize, and rice. Furthermore, SGD1 ubiquitinates the brassinosteroid receptor BRI1, stabilizing it and promoting plant growth. Overexpression of an elite SGD1 haplotype improved grain yield by about 12.8% per plant, and promote complex biological processes such as protein processing in endoplasmic reticulum, stress responses, photosystem stabilization, and nitrogen metabolism. Our research not only identifies the SiUBC32-SGD1-BRI1 genetic module that contributes to grain yield improvement but also provides a strategy for exploring key genes controlling important traits in Poaceae crops using the Setaria model system.

Suggested Citation

  • Sha Tang & Zhiying Zhao & Xiaotong Liu & Yi Sui & Dandan Zhang & Hui Zhi & Yuanzhu Gao & Hui Zhang & Linlin Zhang & Yannan Wang & Meicheng Zhao & Dongdong Li & Ke Wang & Qiang He & Renliang Zhang & We, 2023. "An E2-E3 pair contributes to seed size control in grain crops," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-38812-y
    DOI: 10.1038/s41467-023-38812-y
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    References listed on IDEAS

    as
    1. Xiyu Ma & Lucas A. N. Claus & Michelle E. Leslie & Kai Tao & Zhiping Wu & Jun Liu & Xiao Yu & Bo Li & Jinggeng Zhou & Daniel V. Savatin & Junmin Peng & Brett M. Tyler & Antje Heese & Eugenia Russinova, 2020. "Ligand-induced monoubiquitination of BIK1 regulates plant immunity," Nature, Nature, vol. 581(7807), pages 199-203, May.
    2. Zhi-Yong Wang & Hideharu Seto & Shozo Fujioka & Shigeo Yoshida & Joanne Chory, 2001. "Erratum: BRI1 is a critical component of a plasma-membrane receptor for plant steroids," Nature, Nature, vol. 411(6834), pages 219-219, May.
    3. Sara Martins & Esther M. N. Dohmann & Anne Cayrel & Alexander Johnson & Wolfgang Fischer & Florence Pojer & Béatrice Satiat-Jeunemaître & Yvon Jaillais & Joanne Chory & Niko Geldner & Grégory Vert, 2015. "Internalization and vacuolar targeting of the brassinosteroid hormone receptor BRI1 are regulated by ubiquitination," Nature Communications, Nature, vol. 6(1), pages 1-11, May.
    4. Zhi-Yong Wang & Hideharu Seto & Shozo Fujioka & Shigeo Yoshida & Joanne Chory, 2001. "BRI1 is a critical component of a plasma-membrane receptor for plant steroids," Nature, Nature, vol. 410(6826), pages 380-383, March.
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