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Structural insight into brassinosteroid perception by BRI1

Author

Listed:
  • Ji She

    (Key Laboratory for Protein Sciences of Ministry of Education School of Life Sciences, Tsinghua University
    College of Biological Sciences, Peking University
    National Institute of Biological Sciences, No. 7 Science Park Road, Beijing 102206, China)

  • Zhifu Han

    (Key Laboratory for Protein Sciences of Ministry of Education School of Life Sciences, Tsinghua University)

  • Tae-Wuk Kim

    (Carnegie Institution for Science)

  • Jinjing Wang

    (National Institute of Biological Sciences, No. 7 Science Park Road, Beijing 102206, China)

  • Wei Cheng

    (National Institute of Biological Sciences, No. 7 Science Park Road, Beijing 102206, China)

  • Junbiao Chang

    (Zhengzhou University)

  • Shuai Shi

    (Zhengzhou University)

  • Jiawei Wang

    (Key Laboratory for Protein Sciences of Ministry of Education School of Life Sciences, Tsinghua University)

  • Maojun Yang

    (Key Laboratory for Protein Sciences of Ministry of Education School of Life Sciences, Tsinghua University)

  • Zhi-Yong Wang

    (Carnegie Institution for Science)

  • Jijie Chai

    (Key Laboratory for Protein Sciences of Ministry of Education School of Life Sciences, Tsinghua University
    National Institute of Biological Sciences, No. 7 Science Park Road, Beijing 102206, China)

Abstract

Brassinosteroids are essential phytohormones that have crucial roles in plant growth and development. Perception of brassinosteroids requires an active complex of BRASSINOSTEROID-INSENSITIVE 1 (BRI1) and BRI1-ASSOCIATED KINASE 1 (BAK1). Recognized by the extracellular leucine-rich repeat (LRR) domain of BRI1, brassinosteroids induce a phosphorylation-mediated cascade to regulate gene expression. Here we present the crystal structures of BRI1(LRR) in free and brassinolide-bound forms. BRI1(LRR) exists as a monomer in crystals and solution independent of brassinolide. It comprises a helical solenoid structure that accommodates a separate insertion domain at its concave surface. Sandwiched between them, brassinolide binds to a hydrophobicity-dominating surface groove on BRI1(LRR). Brassinolide recognition by BRI1(LRR) is through an induced-fit mechanism involving stabilization of two interdomain loops that creates a pronounced non-polar surface groove for the hormone binding. Together, our results define the molecular mechanisms by which BRI1 recognizes brassinosteroids and provide insight into brassinosteroid-induced BRI1 activation.

Suggested Citation

  • Ji She & Zhifu Han & Tae-Wuk Kim & Jinjing Wang & Wei Cheng & Junbiao Chang & Shuai Shi & Jiawei Wang & Maojun Yang & Zhi-Yong Wang & Jijie Chai, 2011. "Structural insight into brassinosteroid perception by BRI1," Nature, Nature, vol. 474(7352), pages 472-476, June.
    • Handle: RePEc:nat:nature:v:474:y:2011:i:7352:d:10.1038_nature10178
    DOI: 10.1038/nature10178
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    Cited by:

    1. Teng Jing & Yuying Wu & Yanwen Yu & Jiankun Li & Xiaohuan Mu & Liping Xu & Xi Wang & Guang Qi & Jihua Tang & Daowen Wang & Shuhua Yang & Jian Hua & Mingyue Gou, 2024. "Copine proteins are required for brassinosteroid signaling in maize and Arabidopsis," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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