Csaba Péter, Éva Ádám, Cornelia Klose, Gábor Grézal, Anita Hajdu, Gábor Steinbach, László Kozma-Bognár, Dániel Silhavy, Ferenc Nagy, András Viczián
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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.</p>","PeriodicalId":20575,"journal":{"name":"Plant and Cell Physiology","volume":" ","pages":"1717-1735"},"PeriodicalIF":3.9000,"publicationDate":"2024-11-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11558544/pdf/","citationCount":"0","resultStr":"{\"title\":\"Phytochrome C and Low Temperature Promote the Protein Accumulation and Red-Light Signaling of Phytochrome D.\",\"authors\":\"Csaba Péter, Éva Ádám, Cornelia Klose, Gábor Grézal, Anita Hajdu, Gábor Steinbach, László Kozma-Bognár, Dániel Silhavy, Ferenc Nagy, András Viczián\",\"doi\":\"10.1093/pcp/pcae089\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>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. 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Phytochrome C and Low Temperature Promote the Protein Accumulation and Red-Light Signaling of Phytochrome D.
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.
期刊介绍:
Plant & Cell Physiology (PCP) was established in 1959 and is the official journal of the Japanese Society of Plant Physiologists (JSPP). The title reflects the journal''s original interest and scope to encompass research not just at the whole-organism level but also at the cellular and subcellular levels.
Amongst the broad range of topics covered by this international journal, readers will find the very best original research on plant physiology, biochemistry, cell biology, molecular genetics, epigenetics, biotechnology, bioinformatics and –omics; as well as how plants respond to and interact with their environment (abiotic and biotic factors), and the biology of photosynthetic microorganisms.