Article
Light, phytochrome signalling and photomorphogenesis in Arabidopsis.
IFEVA, Faculty of Agronomy, University of Buenos Aires and National Research Council, Av. San Martín 4453, 1417 Buenos Aires, Argentina.
Photochemical and Photobiological Sciences (impact factor:
2.58).
07/2003;
2(6):625-36.
pp.625-36
Source: PubMed
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Citations (0)
- Cited In (2)
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Article: Light signal transduction in higher plants.
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ABSTRACT: Plants utilize several families of photoreceptors to fine-tune growth and development over a large range of environmental conditions. The UV-A/blue light sensing phototropins mediate several light responses enabling optimization of photosynthetic yields. The initial event occurring upon photon capture is a conformational change of the photoreceptor that activates its protein kinase activity. The UV-A/blue light sensing cryptochromes and the red/far-red sensing phytochromes coordinately control seedling establishment, entrainment of the circadian clock, and the transition from vegetative to reproductive growth. In addition, the phytochromes control seed germination and shade-avoidance responses. The molecular mechanisms involved include light-regulated subcellular localization of the photoreceptors, a large reorganization of the transcriptional program, and light-regulated proteolytic degradation of several photoreceptors and signaling components.Annual Review of Genetics 02/2004; 38:87-117. · 22.23 Impact Factor -
Article: FHY1 mediates nuclear import of the light-activated phytochrome A photoreceptor.
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ABSTRACT: The phytochrome (phy) family of photoreceptors is of crucial importance throughout the life cycle of higher plants. Light-induced nuclear import is required for most phytochrome responses. Nuclear accumulation of phyA is dependent on two related proteins called FHY1 (Far-red elongated HYpocotyl 1) and FHL (FHY1 Like), with FHY1 playing the predominant function. The transcription of FHY1 and FHL are controlled by FHY3 (Far-red elongated HYpocotyl 3) and FAR1 (FAr-red impaired Response 1), a related pair of transcription factors, which thus indirectly control phyA nuclear accumulation. FHY1 and FHL preferentially interact with the light-activated form of phyA, but the mechanism by which they enable photoreceptor accumulation in the nucleus remains unsolved. Sequence comparison of numerous FHY1-related proteins indicates that only the NLS located at the N-terminus and the phyA-interaction domain located at the C-terminus are conserved. We demonstrate that these two parts of FHY1 are sufficient for FHY1 function. phyA nuclear accumulation is inhibited in the presence of high levels of FHY1 variants unable to enter the nucleus. Furthermore, nuclear accumulation of phyA becomes light- and FHY1-independent when an NLS sequence is fused to phyA, strongly suggesting that FHY1 mediates nuclear import of light-activated phyA. In accordance with this idea, FHY1 and FHY3 become functionally dispensable in seedlings expressing a constitutively nuclear version of phyA. Our data suggest that the mechanism uncovered in Arabidopsis is conserved in higher plants. Moreover, this mechanism allows us to propose a model explaining why phyA needs a specific nuclear import pathway.PLoS Genetics 02/2008; 4(8):e1000143. · 8.69 Impact Factor
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Keywords
bind DNA
efficient wavebands
environmental cues
far-red light
induce conformational changes
light signals
nuclear/cytoplasmic partitioning
physical interaction
physiological outputs
phytochrome signalling
phytochrome signalling network
phytochromes
plant photoreceptors
players
versatile relationship