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Plant phytochrome B is an asymmetric dimer with unique signalling potential

Author

Listed:
  • Hua Li

    (Van Andel Institute)

  • E. Sethe Burgie

    (Washington University in St Louis)

  • Zira T. K. Gannam

    (Washington University in St Louis)

  • Huilin Li

    (Van Andel Institute)

  • Richard D. Vierstra

    (Washington University in St Louis)

Abstract

Many aspects of plant photoperception are mediated by the phytochrome (Phy) family of bilin-containing photoreceptors that reversibly interconvert between inactive Pr and active Pfr conformers1,2. Despite extensive biochemical studies, full understanding of plant Phy signalling has remained unclear due to the absence of relevant 3D models. Here we report a cryo-electron microscopy structure of Arabidopsis PhyB in the Pr state that reveals a topologically complex dimeric organization that is substantially distinct from its prokaryotic relatives. Instead of an anticipated parallel architecture, the C-terminal histidine-kinase-related domains (HKRDs) associate head-to-head, whereas the N-terminal photosensory regions associate head-to-tail to form a parallelogram-shaped platform with near two-fold symmetry. The platform is internally linked by the second of two internal Per/Arnt/Sim domains that binds to the photosensory module of the opposing protomer and a preceding ‘modulator’ loop that assembles tightly with the photosensory module of its own protomer. Both connections accelerate the thermal reversion of Pfr back to Pr, consistent with an inverse relationship between dimer assembly and Pfr stability. Lopsided contacts between the HKRDs and the platform create profound asymmetry to PhyB that might imbue distinct signalling potentials to the protomers. We propose that this unique structural dynamism creates an extensive photostate-sensitive surface for conformation-dependent interactions between plant Phy photoreceptors and their signalling partners.

Suggested Citation

  • Hua Li & E. Sethe Burgie & Zira T. K. Gannam & Huilin Li & Richard D. Vierstra, 2022. "Plant phytochrome B is an asymmetric dimer with unique signalling potential," Nature, Nature, vol. 604(7904), pages 127-133, April.
  • Handle: RePEc:nat:nature:v:604:y:2022:i:7904:d:10.1038_s41586-022-04529-z
    DOI: 10.1038/s41586-022-04529-z
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    Cited by:

    1. E. Sethe Burgie & Katherine Basore & Michael J. Rau & Brock Summers & Alayna J. Mickles & Vadim Grigura & James A. J. Fitzpatrick & Richard D. Vierstra, 2024. "Signaling by a bacterial phytochrome histidine kinase involves a conformational cascade reorganizing the dimeric photoreceptor," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    2. Weixiao Yuan Wahlgren & Elin Claesson & Iida Tuure & Sergio Trillo-Muyo & Szabolcs Bódizs & Janne A. Ihalainen & Heikki Takala & Sebastian Westenhoff, 2022. "Structural mechanism of signal transduction in a phytochrome histidine kinase," Nature Communications, Nature, vol. 13(1), pages 1-8, December.
    3. Ruth Jean Ae Kim & De Fan & Jiangman He & Keunhwa Kim & Juan Du & Meng Chen, 2024. "Photobody formation spatially segregates two opposing phytochrome B signaling actions of PIF5 degradation and stabilization," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    4. Juan Du & Keunhwa Kim & Meng Chen, 2024. "Distinguishing individual photobodies using Oligopaints reveals thermo-sensitive and -insensitive phytochrome B condensation at distinct subnuclear locations," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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