ArticlePlant & cell physiology2024
Phytochrome C and Low Temperature Promote the Protein Accumulation and Red-Light Signaling of Phytochrome D.
Article in Plant & cell physiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Blue light as an eco-elicitor effectively enhances flavonoid biosynthesis and antioxidant capacity in dandelion revealed by integrated metabolomic and transcriptomic analyses.BMC plant biology · 2026Article
- A comparative study of femtosecond pulsed and continuous wave lasers on physiological responses through activation of phytochromes in seeds.Scientific reports · 2025Article
- Light regulates the synthesis and accumulation of plant secondary metabolites.Frontiers in plant science · 2025Review
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Authors and funding
10 authors.
Funding
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.
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