Photoresponses of Transgenic Arabidopsis Overexpressing the Fern Adiantum capillus-veneris PHY1

Okamoto, Haruko; Sakamoto, Koji; Tomizawa, Kenji; Nagatani, Akira; Wada, Masamitsu

doi:10.1104/pp.115.1.79

Cited by 20 publications

(5 citation statements)

References 40 publications

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“…The nucleotide sequence of each construct was confirmed by sequencing. All of the constructs were inserted between cauliflower mosaic virus (CaMV) 35S promoter and nopaline synthase (NOS) terminator of pBI H1-IG plasmid vector (36). The Arabidopsis phot1-5 phot2-1 double mutant was transformed with the plasmids described above by the floral-dip method (37) using the Agrobacterium tumefaciens EHA101 strain.…”

Section: Methodsmentioning

confidence: 99%

A single chromoprotein with triple chromophores acts as both a phytochrome and a phototropin

Kanegae

Hayashida

Kuramoto

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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Plants sense their environmental light conditions by using three photoreceptors that absorb in the UV, blue͞near UV, and red͞far-red spectral ranges. These photoreceptors have specific chromophore components corresponding to their absorption spectra. Phytochrome, a red͞far-red light receptor, has phytochromobilin as its chromophore, whereas the blue͞near UV photoreceptors cryptochrome and phototropin have a pair of flavin derivatives. Plants use these various photoreceptors to assess the surrounding light environment. Phytochrome 3 (PHY3) is a red light receptor found in some ferns, which preferentially grow under weak light. PHY3 is composed of a phytochrome chromophore-binding domain in its N-terminal portion and an almost full-length phototropin in its C-terminal half. This unusual domain organization implies that two different light-sensing systems coexist in this single photoreceptor, although these light-sensing systems usually reside in independent photoreceptors. Here, we show that PHY3 acts as a dual-channel photoreceptor that possesses both the red lightsensing system of phytochrome and the blue light-sensing system of phototropin. Furthermore, red-and blue-light signals perceived by PHY3 are processed synergistically within this single chromoprotein. These unusual properties might confer an enhanced light sensitivity on PHY3, allowing ferns to grow under a low-light canopy.fern ͉ phototropism ͉ photoreceptor ͉ red light ͉ blue light P lants have developed sophisticated sensing systems of intensity, direction, duration, and spectral quality of light. Because light consists of components with different wavelengths, plants perceive light signals through various photoreceptors corresponding to wavelength range. These light signals induce various environmental responses of plants and even modulate developmental programs of them (1, 2). Many photomorphogenic responses have been described, for example, control of seed germination, hypocotyl elongation, cotyledon opening, chloroplast development, and gene expression. Among these responses, phototropic response and chloroplast photorelocation movement can be elicited in dicotyledonous plants only by blue͞near UV light (3) and are mediated by phototropins (4). However, in some cryptogamic plants, both phototropic response and chloroplast photorelocation movement are induced by red light (RL) as well as blue light (BL) (5).In the fern Adiantum, both BL-and RL-dependent phototropic responses and chloroplast photorelocation movements are well described (6-9). We showed that these RL-dependent responses of Adiantum are mediated by phytochrome 3 (PHY3) (10). The deduced amino acid sequence indicates that the N-terminal portion of PHY3 contains the chromophore-binding domain of phytochrome, and the C-terminal half shows a remarkable similarity to phototropin (11). The predicted domain organization of PHY3 implies that two different light-sensing systems coexist in this single chromoprotein, although it is not known whether PHY3 can function as a BL receptor or not. I...

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Section: Methodsmentioning

confidence: 99%

A single chromoprotein with triple chromophores acts as both a phytochrome and a phototropin

Kanegae

Hayashida

Kuramoto

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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“…Also nonphotosynthetic eubacteria contain phytochrome-like photoreceptors (23). Among green plants there is a general rule that the absorption wavelength shifts to longer wavelength as taxonomical evolution proceeds (24)(25)(26)(27)(28)(29): the maximum absorption wavelengths of P r and P fr are 665 and 725-730 nm for higher plants, 655 and 720 nm for algae and 649 and 710 nm for moss, respectively. However, those for Physarum are around 680 and 750 nm (Figs.…”

Section: Evolutional Aspects Of the Phytochrome Systems Among Variousmentioning

confidence: 99%

Light Irradiation Induces Fragmentation of the Plasmodium, a Novel Photomorphogenesis in the True Slime Mold Physarum polycephalum: Action Spectra and Evidence for Involvement of the Phytochrome¶

Kakiuchi

Takahashi

Murakami

et al. 2007

Photochemistry and Photobiology

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A new photomorphogenesis was found in the plasmodium of the true slime mold Physarum polycephalum: the plasmodium broke temporarily into equal-sized spherical pieces, each containing about eight nuclei, about 5 h after irradiation with light. Action spectroscopic study showed that UVA, blue and far-red lights were effective, while red light inhibited the far-red-induced fragmentation. Difference absorption spectra of both the living plasmodium and the plasmodial homogenate after alternate irradiation with far-red and red light gave two extremes at 750 and 680 nm, which agreed with those for the induction and inhibition of the fragmentation, respectively. A kinetic model similar to that of phytochrome action explained quantitatively the fluence rate-response curves of the fragmentation. Our results indicate that one of the photoreceptors for the plasmodial fragmentation is a phytochrome.

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“…The T-DNA vector, pBI-HI-BSKR, was used, and the 35S-GUS-NOS terminator region (HindIII-SalI restriction fragment) of T-DNA vector pBI-HI-IG (Okamoto et al, 1997) was replaced with the multi-cloning site (PvuII fragment) from pBluescript SK (1) (Stratagene). A genomic DNA fragment containing At1g75100 was amplified from BAC F9E10 (provided from Arabidopsis Biological Resource Center) by PCR with two primers, 5#-AAGCTTTTAGAGAAAGTAGCTGTCAAT-3# and 5#-GGTACCAGCTTT-AAGTATAAGTTAAGA-3# (underline shows HindIII site and KpnI site, respectively), and was then ligated into the HindIII-KpnI site of the vector (pBI-HI-BSKR-At1g75100).…”

Section: Genetic Mapping and Rescue Of Jac1-1 Mutantmentioning

confidence: 99%

An Auxilin-Like J-Domain Protein, JAC1, Regulates Phototropin-Mediated Chloroplast Movement in Arabidopsis

2005

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The ambient-light conditions mediate chloroplast relocation in plant cells. Under the low-light conditions, chloroplasts accumulate in the light (accumulation response), while under the high-light conditions, they avoid the light (avoidance response). In Arabidopsis (Arabidopsis thaliana), the accumulation response is mediated by two blue-light receptors, termed phototropins (phot1 and phot2) that act redundantly, and the avoidance response is mediated by phot2 alone. A mutant, J-domain protein required for chloroplast accumulation response 1 (jac1), lacks the accumulation response under weak blue light but shows a normal avoidance response under strong blue light. In dark-adapted wild-type cells, chloroplasts accumulate on the bottom of cells. Both the jac1 and phot2 mutants are defective in this chloroplast movement in darkness. Positional cloning of JAC1 reveals that this gene encodes a J-domain protein, resembling clathrin-uncoating factor auxilin at its C terminus. The amounts of JAC1 transcripts and JAC1 proteins are not regulated by light and by phototropins. A green fluorescent protein-JAC1 fusion protein showed a similar localization pattern to green fluorescent protein alone in a transient expression assay using Arabidopsis mesophyll cells and onion (Allium cepa) epidermal cells, suggesting that the JAC1 protein may be a soluble cytosolic protein. Together, these results suggest that JAC1 is an essential component of phototropin-mediated chloroplast movement.

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Photoresponses of Transgenic Arabidopsis Overexpressing the Fern Adiantum capillus-veneris PHY1

Cited by 20 publications

References 40 publications

A single chromoprotein with triple chromophores acts as both a phytochrome and a phototropin

A single chromoprotein with triple chromophores acts as both a phytochrome and a phototropin

Light Irradiation Induces Fragmentation of the Plasmodium, a Novel Photomorphogenesis in the True Slime Mold Physarum polycephalum: Action Spectra and Evidence for Involvement of the Phytochrome¶

An Auxilin-Like J-Domain Protein, JAC1, Regulates Phototropin-Mediated Chloroplast Movement in Arabidopsis

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