Phytochrome C and Low Temperature Promote the Protein Accumulation and Red-Light Signaling of Phytochrome D

Author:

Péter Csaba12,Ádám Éva1,Klose Cornelia3,Grézal Gábor45,Hajdu Anita1,Steinbach Gábor6,Kozma-Bognár László17,Silhavy Dániel1,Nagy Ferenc1,Viczián András1ORCID

Affiliation:

1. Laboratory of Photo and Chronobiology, Institute of Plant Biology, Biological Research Centre, Hungarian Research Network (HUN-REN) , Temesvari krt. 62, Szeged H-6726, Hungary

2. Doctoral School of Biology, Faculty of Sciences and Informatics, University of Szeged , Középfasor 52, Szeged H-6726, Hungary

3. Institute of Biology II, University of Freiburg , Schänzlestr. 1, Freiburg 79104, Germany

4. Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Hungarian Research Network (HUN-REN) , Temesvari krt. 62, Szeged H-6726, Hungary

5. HCEMM-BRC Metabolic Systems Biology Lab , Temesvari krt. 62, Szeged HU-6726, Hungary

6. Cellular Imaging Laboratory, Biological Research Center, Hungarian Research Network (HUN-REN) , Temesvari krt. 62, Szeged H-6726, Hungary

7. Department of Genetics, Faculty of Sciences and Informatics, University of Szeged , Középfasor 52, Szeged H-6726, Hungary

Abstract

Abstract Light affects almost every aspect of plant development. It is perceived by photoreceptors, among which phytochromes (PHY) are responsible for monitoring the red and far-red spectrum. Arabidopsis thaliana possesses five phytochrome genes (phyA–phyE). Whereas functions of phyA and phyB are extensively studied, our knowledge of other phytochromes is still rudimentary. To analyze phyD function, we expressed it at high levels in different phytochrome-deficient genetic backgrounds. Overexpressed phyD-YFP can govern effective light signaling but only at low temperatures and in cooperation with functional phyC. Under these conditions, phyD-YFP accumulates to high levels, and opposite to phyB, this pool is stable in light. By comparing the photoconvertible phyD-YFP and phyB levels and their signaling in continuous and pulsed irradiation, we showed that phyD-YFP is a less efficient photoreceptor than phyB. This conclusion is supported by the facts that only a part of the phyD-YFP pool is photoconvertible and that thermal reversion of phyD-YFP is faster than that of phyB. Our data suggest that the temperature-dependent function of phyD is based on the amount of phyD protein and not on its Pfr stability, as described for phyB. We also found that phyD-YFP and phyB-GFP are associated with strongly overlapping genomic locations and are able to mediate similar changes in gene expression; however, the efficiency of phyD-YFP is lower. Based on these data, we propose that under certain conditions, synergistic interaction of phyD and phyC can substitute phyB function in seedlings and in adult plants and thus increases the ability of plants to respond more flexibly to environmental changes.

Funder

Hungarian Scientific Research Fund

Publisher

Oxford University Press (OUP)

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