| Missense Mutation in the N Terminal of Phytochrome A Disrupts the Nuclear Import of the Photoreceptor. | |
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MedLine Citation:
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PMID: 21969386 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Phytochromes are the red/far-red photoreceptors in higher plants. Among them phytochrome A (PHYA) is responsible for the far-red high irradiance response (HIR) and for the perception of very low amounts of light, initiating the very low fluence response (VLFR). Here we report a detailed physiological and molecular characterization of the phyA-5 mutant which displays hyposensitivity to continuous low-intensity far-red light and shows reduced VLFR and HIR. Red light-induced degradation of the mutant phyA-5 protein appears to be normal, yet higher residual amounts of phyA-5 are detected in seedlings grown under low-intensity far-red light. We show that (i) the phyA-5 mutant harbors a new missense mutation in the PHYA amino terminal extension (NTE) domain and that (ii) the complex phenotype of the mutant is caused by reduced nuclear import of phyA-5 under low fluences of far-red light. We also demonstrate that impaired nuclear import of phyA-5 is brought about by weakened binding affinity of the mutant photoreceptor to nuclear import facilitators FHY1 (for FAR-RED ELONGATED HYPOCOTYL1) and FHL (for FHY1-LIKE). Finally, we provide evidence that signaling and degradation kinetics of constitutively nuclear localized phyA-5 and phyA are identical. Taken together, our data show that aberrant nucleo/cytoplasmic distribution impairs light-induced degradation of this photoreceptor, the NTE domain mediates formation of the FHY1/FHL/PHYA Pfr complex, thereby it plays a role in regulating nuclear import of phyA. |
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Authors:
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Vladyslava Sokolova; János Bindics; Stefan Kircher; Eva Adám; Eberhard Schäfer; Ferenc Nagy; András Viczián |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-10-3 |
Journal Detail:
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Title: Plant physiology Volume: - ISSN: 1532-2548 ISO Abbreviation: - Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-10-4 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0401224 Medline TA: Plant Physiol Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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1 Institute of Plant Biology, Biological Research Centre of the Hungarian Academy of Sciences, Szeged,; |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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