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Plant Phytochrome Interactions Decode Light and Temperature Signals

Titelangaben

Yi, Chengwei ; Gerken, Uwe ; Tang, Kun ; Philipp, Michael ; Zurbriggen, Matias D. ; Köhler, Jürgen ; Möglich, Andreas:
Plant Phytochrome Interactions Decode Light and Temperature Signals.
In: The Plant Cell. (September 2024) . - koae249.
ISSN 1532-298X
DOI: https://doi.org/10.1093/plcell/koae249

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Abstract

Plant phytochromes perceive red and far-red light to elicit adaptations to the changing environment. Downstream physiological responses revolve around red-light-induced interactions with phytochrome-interacting factors (PIF). Phytochromes double as thermoreceptors, owing to the pronounced temperature dependence of thermal reversion from the light-adapted Pfr to the dark-adapted Pr state. Here, we assess whether thermoreception may extend to the phytochrome:PIF interactions. While the association between Arabidopsis (Arabidopsis thaliana) PHYTOCHROME B (PhyB) and several PHYTOCHROME-INTERACTING FACTOR (PIF) variants moderately accelerates with temperature, the dissociation does more so, thus causing net destabilization of the phytochrome:PIF complex. Markedly different temperature profiles of PIF3 and PIF6 might underlie stratified temperature responses in plants. Accidentally, we identify a photoreception mechanism under strong continuous light, where the extent of phytochrome:PIF complexation decreases with red-light intensity rather than increases. Mathematical modeling rationalizes this attenuation mechanism and ties it to rapid red-light-driven Pr⇄Pfr interconversion and complex dissociation out of Pr. Varying phytochrome abundance, e.g., during diurnal and developmental cycles, and interaction dynamics, e.g., across different PIFs, modify the nature and extent of attenuation, thus permitting light-response profiles more malleable than possible for the phytochrome Pr⇄Pfr interconversion alone. Our data and analyses reveal a photoreception mechanism with implications for plant physiology, optogenetics, and biotechnological applications.

Weitere Angaben

Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Institutionen der Universität: Fakultäten > Fakultät für Mathematik, Physik und Informatik > Physikalisches Institut > Lehrstuhl Experimentalphysik IX - Spektroskopie weicher Materie > Lehrstuhl Experimentalphysik IX - Spektroskopie weicher Materie - Univ.-Prof. Dr. Jürgen Köhler
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Lehrstuhl Biochemie II - Photobiochemie > Lehrstuhl Biochemie II - Photobiochemie - Univ.-Prof. Dr. Andreas Möglich
Titel an der UBT entstanden: Ja
Themengebiete aus DDC: 500 Naturwissenschaften und Mathematik > 570 Biowissenschaften; Biologie
Eingestellt am: 24 Sep 2024 06:28
Letzte Änderung: 24 Sep 2024 06:28
URI: https://eref.uni-bayreuth.de/id/eprint/90474