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Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling

Author

Listed:
  • Elina Multamäki

    (University of Helsinki)

  • Rahul Nanekar

    (University of Jyvaskyla)

  • Dmitry Morozov

    (University of Jyvaskyla)

  • Topias Lievonen

    (University of Jyvaskyla)

  • David Golonka

    (Lehrstuhl für Biochemie, Universität Bayreuth)

  • Weixiao Yuan Wahlgren

    (Department of Chemistry and Molecular Biology, University of Gothenburg)

  • Brigitte Stucki-Buchli

    (University of Jyvaskyla)

  • Jari Rossi

    (University of Helsinki)

  • Vesa P. Hytönen

    (Tampere University
    Fimlab Laboratories)

  • Sebastian Westenhoff

    (Department of Chemistry and Molecular Biology, University of Gothenburg)

  • Janne A. Ihalainen

    (University of Jyvaskyla)

  • Andreas Möglich

    (Lehrstuhl für Biochemie, Universität Bayreuth)

  • Heikki Takala

    (University of Helsinki
    University of Jyvaskyla)

Abstract

Bacterial phytochrome photoreceptors usually belong to two-component signaling systems which transmit environmental stimuli to a response regulator through a histidine kinase domain. Phytochromes switch between red light-absorbing and far-red light-absorbing states. Despite exhibiting extensive structural responses during this transition, the model bacteriophytochrome from Deinococcus radiodurans (DrBphP) lacks detectable kinase activity. Here, we resolve this long-standing conundrum by comparatively analyzing the interactions and output activities of DrBphP and a bacteriophytochrome from Agrobacterium fabrum (Agp1). Whereas Agp1 acts as a conventional histidine kinase, we identify DrBphP as a light-sensitive phosphatase. While Agp1 binds its cognate response regulator only transiently, DrBphP does so strongly, which is rationalized at the structural level. Our data pinpoint two key residues affecting the balance between kinase and phosphatase activities, which immediately bears on photoreception and two-component signaling. The opposing output activities in two highly similar bacteriophytochromes suggest the use of light-controllable histidine kinases and phosphatases for optogenetics.

Suggested Citation

  • Elina Multamäki & Rahul Nanekar & Dmitry Morozov & Topias Lievonen & David Golonka & Weixiao Yuan Wahlgren & Brigitte Stucki-Buchli & Jari Rossi & Vesa P. Hytönen & Sebastian Westenhoff & Janne A. Iha, 2021. "Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling," Nature Communications, Nature, vol. 12(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24676-7
    DOI: 10.1038/s41467-021-24676-7
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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.

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