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Gibberellin-induced DELLA recognition by the gibberellin receptor GID1

Author

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  • Kohji Murase

    (Structural Biology Laboratory, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan
    Duke University, Durham, North Carolina 27708, USA)

  • Yoshinori Hirano

    (Structural Biology Laboratory, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan)

  • Tai-ping Sun

    (Duke University, Durham, North Carolina 27708, USA)

  • Toshio Hakoshima

    (Structural Biology Laboratory, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan)

Abstract

Gibberellins control a range of growth and developmental processes in higher plants and have been widely used in the agricultural industry. By binding to a nuclear receptor, GIBBERELLIN INSENSITIVE DWARF1 (GID1), gibberellins regulate gene expression by promoting degradation of the transcriptional regulator DELLA proteins, including GIBBERELLIN INSENSITIVE (GAI). The precise manner in which GID1 discriminates and becomes activated by bioactive gibberellins for specific binding to DELLA proteins remains unclear. Here we present the crystal structure of a ternary complex of Arabidopsis thaliana GID1A, a bioactive gibberellin and the amino-terminal DELLA domain of GAI. In this complex, GID1A occludes gibberellin in a deep binding pocket covered by its N-terminal helical switch region, which in turn interacts with the DELLA domain containing DELLA, VHYNP and LExLE motifs. Our results establish a structural model of a plant hormone receptor that is distinct from the mechanism of the hormone perception and effector recognition of the known auxin receptors.

Suggested Citation

  • Kohji Murase & Yoshinori Hirano & Tai-ping Sun & Toshio Hakoshima, 2008. "Gibberellin-induced DELLA recognition by the gibberellin receptor GID1," Nature, Nature, vol. 456(7221), pages 459-463, November.
    • Handle: RePEc:nat:nature:v:456:y:2008:i:7221:d:10.1038_nature07519
    DOI: 10.1038/nature07519
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    Cited by:

    1. Jia Zhou & Qinli Hu & Xinlong Xiao & Deqiang Yao & Shenghong Ge & Jin Ye & Haojie Li & Rujie Cai & Renyang Liu & Fangang Meng & Chao Wang & Jian-Kang Zhu & Mingguang Lei & Weiman Xing, 2021. "Mechanism of phosphate sensing and signaling revealed by rice SPX1-PHR2 complex structure," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    2. Mohamed Mahameed & Pengli Wang & Shuai Xue & Martin Fussenegger, 2022. "Engineering receptors in the secretory pathway for orthogonal signalling control," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    3. Yage Ding & Cristina Tous & Jaehoon Choi & Jingyao Chen & Wilson W. Wong, 2024. "Orthogonal inducible control of Cas13 circuits enables programmable RNA regulation in mammalian cells," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    4. Xu Huang & Rodolfo Zentella & Jeongmoo Park & Larry Reser & Dina L. Bai & Mark M. Ross & Jeffrey Shabanowitz & Donald F. Hunt & Tai-ping Sun, 2024. "Phosphorylation activates master growth regulator DELLA by promoting histone H2A binding at chromatin in Arabidopsis," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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