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Structural mechanism of signal transduction in a phytochrome histidine kinase

Author

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  • Weixiao Yuan Wahlgren

    (University of Gothenburg)

  • Elin Claesson

    (University of Gothenburg)

  • Iida Tuure

    (University of Jyvaskyla)

  • Sergio Trillo-Muyo

    (University of Gothenburg)

  • Szabolcs Bódizs

    (University of Gothenburg)

  • Janne A. Ihalainen

    (University of Jyvaskyla)

  • Heikki Takala

    (University of Jyvaskyla
    University of Helsinki)

  • Sebastian Westenhoff

    (University of Gothenburg
    Uppsala University)

Abstract

Phytochrome proteins detect red/far-red light to guide the growth, motion, development and reproduction in plants, fungi, and bacteria. Bacterial phytochromes commonly function as an entrance signal in two-component sensory systems. Despite the availability of three-dimensional structures of phytochromes and other two-component proteins, the conformational changes, which lead to activation of the protein, are not understood. We reveal cryo electron microscopy structures of the complete phytochrome from Deinoccocus radiodurans in its resting and photoactivated states at 3.6 Å and 3.5 Å resolution, respectively. Upon photoactivation, the photosensory core module hardly changes its tertiary domain arrangement, but the connector helices between the photosensory and the histidine kinase modules open up like a zipper, causing asymmetry and disorder in the effector domains. The structures provide a framework for atom-scale understanding of signaling in phytochromes, visualize allosteric communication over several nanometers, and suggest that disorder in the dimeric arrangement of the effector domains is important for phosphatase activity in a two-component system. The results have implications for the development of optogenetic applications.

Suggested Citation

  • 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.
  • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-34893-3
    DOI: 10.1038/s41467-022-34893-3
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    References listed on IDEAS

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    1. Jeremiah R. Wagner & Joseph S. Brunzelle & Katrina T. Forest & Richard D. Vierstra, 2005. "A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome," Nature, Nature, vol. 438(7066), pages 325-331, November.
    2. 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.
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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. Stefanie S. M. Meier & Elina Multamäki & Américo T. Ranzani & Heikki Takala & Andreas Möglich, 2024. "Leveraging the histidine kinase-phosphatase duality to sculpt two-component signaling," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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