Pr and Pfr structures of plant phytochrome A

Phytochromes are biliprotein photoreceptors widespread amongst microorganisms and ubiquitous in plants where they control developmental processes as diverse as germination, stem elongation and floral induction through the photoconversion of inactive Pr to the Pfr signalling state. Here we report crystal structures of the chromophore-binding module of soybean phytochrome A, including ~2.2 Å XFEL structures of Pr and Pfr at ambient temperature and high resolution cryogenic structures of Pr. In the Pfr structure, the chromophore is exposed to the medium, the D-ring remaining α-facial following the likely clockwise photoflip. The chromophore shifts within its pocket, while its propionate side chains, their partners as well as three neighbouring tyrosines shift radically. Helices near the chromophore show substantial shifts that might represent components of the light signal. These changes reflect those in bacteriophytochromes despite their quite different signalling mechanisms, implying that fundamental aspects of phytochrome photoactivation have been repurposed for photoregulation in the eukaryotic plant.

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Publication Details

Journal
Nature Communications
Published
2025-06-21
DOI
https://doi.org/10.1038/s41467-025-60738-w
Citations
7
Primary Topic
Light effects on plants
Type
article
Field-Weighted Citation Impact
12.25

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article

Pr and Pfr structures of plant phytochrome A

Tokushi Sato, Chen Song, Raphaël de Wijn, Christina Schmidt et al.
7 citations
Nature Communications
Light effects on plants
12.25
article

Pr and Pfr structures of plant phytochrome A

Tokushi Sato, Chen Song, Raphaël de Wijn, Christina Schmidt, Joana Valério, Huijong Han, Agnieszka Wrona, Jayanath Koliyadu, Lea Brings, Joachim Schulz, Johan Bielecki, David von Stetten, Adrian P. Mancuso⋈, F. Koua, Kaoling Guan, Jon Hughes, Thomas R. M. Barends, S. Nagano, Peng-Yuan Chen, C. Feiler, Romain Letrun, Richard Bean, M.S. Weiss, Abhisakh Sarma, Iñaki de Diego, Konstantin Kharitonov, Karsten Heyne, Robin Schubert, Katerina Dörner, Marco Kloos, Chan Kim, Ekaterina Round
article en
7 citations

Abstract

Phytochromes are biliprotein photoreceptors widespread amongst microorganisms and ubiquitous in plants where they control developmental processes as diverse as germination, stem elongation and floral induction through the photoconversion of inactive Pr to the Pfr signalling state. Here we report crystal structures of the chromophore-binding module of soybean phytochrome A, including ~2.2 Å XFEL structures of Pr and Pfr at ambient temperature and high resolution cryogenic structures of Pr. In the Pfr structure, the chromophore is exposed to the medium, the D-ring remaining α-facial following the likely clockwise photoflip. The chromophore shifts within its pocket, while its propionate side chains, their partners as well as three neighbouring tyrosines shift radically. Helices near the chromophore show substantial shifts that might represent components of the light signal. These changes reflect those in bacteriophytochromes despite their quite different signalling mechanisms, implying that fundamental aspects of phytochrome photoactivation have been repurposed for photoregulation in the eukaryotic plant.

Nature CommunicationsVol. 16(1)
Justus-Liebig-Universität Gießen (DE), Helmholtz-Zentrum Berlin für Materialien und Energie (DE), Diamond Light Source (GB), Max Planck Institute for Medical Research (DE), European Molecular Biology Laboratory (DE), Freie Universität Berlin (DE), The University of Texas at Austin (US), European X-Ray Free-Electron Laser (DE), Leipzig University (DE)
Deutsche Forschungsgemeinschaft, Bundesministerium für Bildung und Forschung, Universität Hamburg, Helmholtz-Zentrum Berlin für Materialien und Energie, Deutsches Elektronen-Synchrotron
Life in Land
Openalex Percentile: Top 2%
Light effects on plants
12.25
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