• Molecules and Cells
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• v.38 no.7
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• pp.651-656
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• 2015

Plant growth and development are coordinately orchestrated by environmental cues and phytohormones. Light acts as a key environmental factor for fundamental plant growth and physiology through photosensory phytochromes and underlying molecular mechanisms. Although phytochromes are known to possess serine/threonine protein kinase activities, whether they trigger a signal transduction pathway via an intracellular protein kinase network remains unknown. In analyses of mitogen-activated protein kinase kinase (MAPKK, also called MKK) mutants, the mkk3 mutant has shown both a hypersensitive response in plant hormone gibberellin (GA) and a less sensitive response in red light signaling. Surprisingly, light-induced MAPK activation in wild-type (WT) seedlings and constitutive MAPK phosphorylation in dark-grown mkk3 mutant seedlings have also been found, respectively. Therefore, this study suggests that MKK3 acts in negative regulation in darkness and in light-induced MAPK activation during dark-light transition.

• Interdisciplinary Bio Central
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• v.1 no.1
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• pp.1.1-1.5
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• 2009

Many organisms control their physiology and behavior in response to the local light environment, which is first perceived by photoreceptors that undergo light-dependent conformational changes. Phytochromes are one of the major photoreceptors in plants, controlling wide aspects of plant physiology by recognizing the light in red (R) and far-red (FR) spectra. Higher plants have two types of phytochromes; the photo-labile type I (phyA in Arabidopsis) and photo-stable type II (phyB-E in Arabidopsis). Phytochrome B (phyB), a member of the type II phytochromes in Arabidopsis, shows classical R and FR reversibility between the inter-convertible photoisomers, Pr and Pfr. Interestingly, the Pr and Pfr isomers show partitioning in the cytosol and nucleus, respectively. In the over 50 years since its discovery, it has been thought that the type II phytochromes only function to mediate R light. As described in the text, we have now discovered phyB has an active function in FR light. Even striking is that the R and FR light exert an opposite effect. Thus, FR light is not simply nullifying the R effect but has an opposing effect to R light. What is more interesting is that the phyB-mediated actions of FR and R light occur at different cellular compartment of the plant cell, cytosol and nucleus, respectively, which was proven through utilization of the cytosolic and nuclear-localized mutant versions of phyB. Our observations thus shoot down a major dogma in plant physiology and will be considered highly provocative in phytochrome function. We argue that it would make much more sense that plants utilize the two isoforms rather than only one form, to effectively monitor the changing environmental light information and to incorporate the information into their developmental programs.

• Proceedings of the Korean Society of Plant Biotechnology Conference
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• 2004.10a
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• pp.45-45
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• 2004

• Proceedings of the Botanical Society of Korea Conference
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• 1996.06a
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• pp.10-17
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• 1996

Fern gametophytes are a good model system to study plant morphogenesis, because of their simple organization and various photocontrolled responses. We studied fern photomorphogenesis including chloroplast photoorientation using Adiantum gametophytes to analyze signal transduction pathways of plant photomorphogenesis. Chloroplast photoorientation will be shown in detail and molecular structure of fern phytochromes and blue light absorbing pigments will also be discussed.

• Proceedings of the Korean Society of Potoscience Conference
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• 2005.06a
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• pp.33-34
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• 2005

• Applied Biological Chemistry
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• v.32 no.2
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• pp.126-131
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• 1989

Binding properties of the degraded 59kD phytochrome from etiolated Avena sativa seedlings to liposomes and Cibacron Blue dye were examined. In contrast with the native 124kD and partially degraded 118kD phytochromes, the farred light absorbing(Pfr) forms of the 59kD phytochrome binds to liposomes and Cibacron Blue dye via electrostatic interactions. Results indicate that the 59kD Pfr does not hold a hydrophobic surface which is exposed upon Pr to Pfr phototransformation of the 124 and 118kD phytochromes. Since a relatively extensive hydrophobic region is located in the chromophore bearing domain(59kD) of phytochrome(Hershey et al., Nuc. Acids Res., 13, 8543, 1986), the 55kD tryptic domain from the C-terminus plays an important role on the exposure of the hydrophobic area in the 118 and 124 Pfr to occur.

• Journal of Life Science
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• v.28 no.1
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• pp.9-16
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• 2018

Light is essential to the growth and development of plants, and it is perceived by phytochromes, which are one of the photoreceptors that regulate physiological responses in plants. Ethylene regulates the dormancy, senescence, growth, and development of organs in plants. This research focused on the interaction of phytochromes and ethylene to control hypocotyl growth and gravitropism using phytochrome mutants of Arabidopsis, phyA, phyB, and phyAB, under three light conditions: red (R) light, farred (FR) light, and white light. The mutant phyAB exhibited the most stimulation of gravitropic response of all three phytochrome mutants and wild type (WT) in all three light conditions. Moreover, phyB in the R light condition showed more negative gravitropism than phyA. However, phyB in the FR light condition showed less curvature than phyA. The hypocotyl growth pattern was similar to the gravitropic response in several light conditions. To explain the mechanism of the regulation of gravitropic response and growth, we measured the ethylene production and activities of in vitro ACS and ACO. Ethylene production was reduced in all the mutants grown in white light in comparison to the WT. Ethylene production increased in the phyA grown in R light and phyB grown in FR light in comparison to the other mutants. The ACS activity coincided with the ethylene production in the phyA and the phyB grown in R light and FR light, respectively. These results suggest that the Pfr form of phyB in R light and the Pr form of phyA in FR light increased ethylene production via increasing ACS activity.

• Proceedings of the Microbiological Society of Korea Conference
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• 2005.05a
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• pp.64-66
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• 2005

Photosynthetic microbes possess a wealth of photoactive proteins including chlorophyll-based pigments, phototropin-related blue light receptors, phytochromes, and cryptochromes. Surprisingly, recent genome sequencing projects discovered additional photoactive proteins, retinal-based rhodopsins, in cyanobacterial and algal genera. Most of these newly found rhodopsin genes and retinal synthase have not been expressed and their functions are unknown. Analysis of the Anabaena and Chlamyrhodopsin with retinal synthase revealed that they have sensory functions, which, based on our work with haloarchaeal rhodopsins, may use a variety of signaling mechanisms. Anabaena rhodopsin is believed to be sensory, shown to interact with a soluble transducer and the putative function is either chromatic adaptation or circadian rhythm. Chlamydomonas rhodopsins are involved in phototaxis and photophobic responses based on electrical measurements by RNAi experiment. In order to analyze the protein, we developed a sensory rhodopsin expression system in E. coli. The opsin in E. coil bound endogenous all-trans retinal to form a pigment and can be observed on the plate. Using this system we could identify retinal synthase in Anabaena PCC 7120. We conclude that Anabaena D475 dioxygenase functions as a retinal synthase to the Anabaena rhodopsin in the cell.

• Journal of Photoscience
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• v.10 no.1
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• pp.157-164
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• 2003

Light exerts two primary roles in plant growth and development. Plants acquire all biochemical energy required for growth and propagation solely from light energy via photosynthesis. In addition, light serves as a medium through which plants recognize environmental fluctuations, such as photoperiod and presence of neighboring animals and plants. Plants therefore constantly monitor the direction, intensity, duration, and wavelength of environmental light and integrate these light signals into the intrinsic regulatory programs to achieve an optimized growth in a given light condition. Although light regulates all aspects of plant growth and developmental aspects, the molecular mechanisms and signaling cascades involved have not been well established until recently. However, recent advances in genetic tools and plant transformation techniques greatly facilitated the elucidation of molecular events in plant photomorphogenesis. This mini-review summarizes the gist of recent findings in deetiolation and suppression of shade avoidance response as classic examples of the phytochrome-mediated photomorphogenesis.

• Journal of Photoscience
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• v.9 no.2
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• pp.90-93
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• 2002

Phytochrome A (phyA) and phytochrome B (phyB) perceive light and adapt to fluctuating circumstances by different manners in terms of effective wavelengths, required fluence and photoreversibility. Action spectra for induction of seed germination and inhibition of hypocotyl elongation using phytochrome mutants of Arabidopsis showed major difference. PhyA is the principal photoreceptor for the very low fluence responses and the far-red light-induced high irradiance responses, while phyB controls low fluence response in a red/far-red reversible mode. The structural requirement of their bilin chromophores for photosensory specificity of phyA and phyB was investigated by reconstituting holophytochromes through feeding various synthetic bilins to the following chromophore-deficient mutants: hy1, hyl/phyA and hyl/phyB mutants of Arabidopsis. We found that the vinyl side-chain of the D-ring in phytochromobilin interacts with phyA apoprotein. This interaction plays a direct role in mediating the specific photosensory function of phyA. The ethyl side-chain of the D-ring in phycocyanobilin fails to interact with phyA apoprotein, therefore, phyA specific photosensory function is not observed. In contrast, both phytochromobilin and phycocyanobilin interact with phyB apoprotein and induce phyB specific photosensory functions. Structural requirements of the apoproteins and the chromophores for the specific photoperception of phyA and phyB are discussed.