Cited by 114Light effects on plantsPlant Molecular Biology ResearchPlant Parasitism and Resistance

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Arabidopsis fhl / fhy1 double mutant reveals a distinct cytoplasmic action of phytochrome A

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Rösler, Jutta, Klein, Ilse, Zeidler, Mathias·2007·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0703855104PMC PMC1965582

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Abstract

Phytochrome A (phyA) plays an important role during germination and early seedling development. Because phyA is the primary photoreceptor for the high-irradiance response and the very-low-fluence response, it can trigger development not only in red and far-red (FR) light but also in a wider range of light qualities. Although phyA action is generally associated with translocation to the nucleus and regulation of transcription, there is evidence for additional cytoplasmic functions. Because nuclear accumulation of phyA has been shown to depend on far-red-elongated hypocotyl 1 (FHY1) and FHL (FHY1-like), investigation of phyA function in a double fhl/fhy1 mutant might be valuable in revealing the mechanism of phyA translocation and possible cytoplasmic functions. In fhl/fhy1 , the FR-triggered nuclear translocation of phyA could no longer be detected but could be restored by transgenic expression of CFP:FHY1 . Whereas the fhl/fhy1 mutant showed a phyA phenotype in respect to hypocotyl elongation and cotyledon opening under high-irradiance response conditions as well as a typical phyA germination phenotype under very-low-fluence response conditions, fhl/fhy1 showed no phenotype with respect to the phyA-dependent abrogation of negative gravitropism in blue light and in red-enhanced phototropism, demonstrating clear cytoplasmic functions of phyA. Disturbance of phyA nuclear import in fhl/fhy1 led to formation of FR-induced phyA:GFP cytoplasmic foci resembling the sequestered areas of phytochrome. FHY1 and FHL play crucial roles in phyA nuclear translocation and signaling. Thus the double-mutant fhl/fhy1 allows nuclear and cytoplasmic phyA functions to be separated, leading to the novel identification of cytoplasmic phyA responses.

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Authors: Rösler, J., Klein, I., & Zeidler, M.
Affiliations: Justus-Liebig-Universität Gießen (DE)
Carnegie Institution for Science (US)
Corresponding author: Zeidler, Mathias
ORCID: Zeidler, Mathias
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2007-06-19
Volume: 104
Issue: 25
Pages: 10737-10742
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.0703855104
PMC: PMC1965582
OpenAlex: W2096295687
Cited by: 114
References: 47
Citations by year: 2026: 3 · 2025: 7 · 2023: 4 · 2022: 5 · 2021: 5 · 2020: 3 · 2019: 4 · 2018: 7 · 2017: 1 · 2016: 4 · 2015: 3 · 2014: 10 · 2013: 8 · 2012: 13
FWCI: 10.94
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Deutsche Forschungsgemeinschaft
Topics: Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Parasitism and Resistance
Keywords: phytochrome A, nuclear translocation, far-red light, high irradiance response, hypocotyl elongation, cotyledon opening, gravitropism, phototropism, Arabidopsis thaliana, double mutants
MeSH terms: Cytoplasm, Mutation, Recombinant Fusion Proteins, Arabidopsis, Hypocotyl, Transgenes, Arabidopsis Proteins, Plants, Genetically Modified, Green Fluorescent Proteins, Phytochrome A

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Arabidopsis fhl / fhy1 double mutant reveals a distinct cytoplasmic action of phytochrome A

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