• BMB Reports
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• v.31 no.3
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• pp.221-226
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• 1998

Phosphorylation of phytochrome may play important functional roles to control plant photomorphogenesis. Many attempts have failed to identify the protein kinase that phosphorylates phytochrome in vivo. It has been reported that a polycation-stimulated protein kinase activity was associated with the purified phytochrome. However, it is not known if the kinase activity is an intrinsic property of phytochrome or whether it comes from a contaminant of the purified phytochrome. In the present study, three protein kinases that phosphorylate phytochrome have been identified from etiolated oat seedlings. A polycationstimulated protein kinase that had very similar enzymatic properties with that associated with the purified phytochrome was identified in the cytosolic extract. It phosphorylated several contaminant proteins in the kinase preparation as well as phytochrome and had a broad substrate specificity. A CK II-type protein kinase phosphorylated phytochrome and the exogenously added casein. It is likely that this kinase may not be a feasible candidate for the kinase phosphorylating phytochrome in vivo since the content of the kinase seemed to well exceed the content of phytochrome in the etiolated oat seedlings. Another protein kinase that had unique enzymatic properties phosphorylated phytochrome very specifically and seemed to be present in a small quantity in the etiohlted seedlings. It is expected that one of three kinases may be responsible for the phytochrome phosphorylation in vivo.

• Rapid Communication in Photoscience
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• v.2 no.2
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• pp.56-59
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• 2013

Plant phytochromes, molecular light switches that regulate various aspects of plant growth and development, are known as autophosphorylating serine/threonine kinases. Although recent studies reveal that phytochrome autophosphorylation plays an important role in the regulation of phytochrome signaling through the control of phyA protein stability, the in vivo functional roles of phytochrome kinase activity in plant light signaling are largely unknown. Thus, it is necessary to investigate the detailed function of phytochrome as a protein kinase, which might include mapping of kinase domain on the phytochrome molecule, searching for substrates that could be phosphorylated by phyA, and in vivo functional analysis of the kinase activity with phytochrome mutants displaying reduced kinase activity. Our recent studies reveal that the kinase activity of phytochrome plays a positive role in plant light signaling. Therefore, we highlight the current knowledge about the functional roles of phytochrome kinase activity in the light signal transduction of plants, based on our recent results.

• 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.

• Proceedings of the Botanical Society of Korea Conference
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• 1994.09a
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• pp.41-51
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• 1994

Tomato (Lycopersicon esculentum Mill.) has been chosen as a model species for the study of hotomorphogenesis. The aurea (au) and yellow-green-2 (yg-2) mutants which are severely photochrome deficient appear to be phytochrome chromophore mutants. Mutants modified with respect to specific members of the phytochrome gene family: the far-red light-insensitive mutant (fri, for phytochrome A) and the temporarily red light-insensitive mutant (tri, for phytochrome B1) have been identified. Mutants that exhibit an exaggerated phytochrome response are putative transduction-chain mutants affecting an amplification step in phytochrome signal transduction. These mutants are being used to understand the complexities of juvenile anthocyanin in the hypocotyl during seedling de-etiolation.

• Journal of Microbiology and Biotechnology
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• v.16 no.9
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• pp.1441-1447
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• 2006

The light perception and phototransformation of phytochromes are the first process of the phytochrome-mediated light signal transduction. The chromophore ligation and its photochromism of various site-specific and deletion mutants of pea phytochrome A and bacterial phytochrome-like protein (Cph1) were analyzed in vitro. Serial truncation mutants from the N-terminus and C-terminus indicated that the minimal N-terminal domain for the chromophore ligation spans from the residue 78 to 399 of pea phytochrome A. Site-specific mutants indicated that several residues are critical for the chromophore ligation and/or photochromism. Histidine-324 appears to serve as an anchimeric residue for photochromism through its H-bonding function. Isoleucine-80 and arginine-383 playa critical role for the chromophore ligation and photochromism. Arginine-383 is presumably involved in the stabilization of the Pfr form of pea phytochrome A. Apparently, the amphiphilic ${\alpha}$-helix centered around the residue-391 is in the chromophore pocket and critical for the chromophore ligation.

• Journal of Photoscience
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• v.7 no.3
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• pp.123-128
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• 2000

Phosphorylation of cellular proteins is a key regulatory mehanism for signal transduction pathway in living cells. Phytochrome, a red/far-red light photoreceptor in plants, is known to employ protein phosphorylation for its light signaling, although its detauked mechanism is still ambiguous. This study is intended to identify the phosphoproteins and protein kinases that are regulated by phytochrome, by employing transgenic rice seedlings that overexpress Arabidopsis phytochrome A. Red light stimulated phsophorylation of a 70 kDa protein and far-red light negated the effect. The red light induced phosphotylation of the 70 kDa protein was strongly activated by heparin and inhibited by poly-L-lysine, suggesting that the 70 kDa protein phosphorylating kinase belongs to GSK-3/SHAGGY protein kinase that has functional roles in establishing cell fate and pattern formation in Drosophila. Taken together with the fact that phytochrome controls plant development, these results may suggest that a GSK-3/SHAGGY-related protein kinase in plant(ASK) is likely to be involved in phytochrome signal transduction.

• Bulletin of the Korean Chemical Society
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• v.8 no.4
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• pp.347-348
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• 1987

• Journal of Korean Society of Forest Science
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• v.94 no.4 s.161
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• pp.236-242
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• 2005

Phytochrome B (PhyB) gene, which is a photoreceptor that controls plant growth under various light conditions, was cloned from Chinese hybrid poplar 'Soohang 1'. Nucleotide sequence and deduced amino acid sequences PhyB cDNA of 'Soohang' is consisted with 3,456 nucleotides and 1,156 amino acids. The cloned PhyB fragment showed 98% homology of amino acid sequences with Populus balsamifera PhyB1. According to Northern blot analysis. PhyB was up-regulated by light, while PhyB transcript was not detected under dark condition. According to this study, the cloned PhyB is induced by light and functions as photoreceptor.

• Journal of Photoscience
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• v.9 no.2
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• pp.338-340
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• 2002

In broom sorghum, Sorghum bicolor Moench, UV causes anthocyanin synthesis having action peaks in UVA and UVB regions. We previously reported that UV induces anthocyanin synthesis through UVB photoreceptor and phytochrome activated by UV. Furthermore, UVA and UVB amplify phytochrome-induced anthocyanin synthesis (PIAS). Our action- spectroscopic research indicated that a UV -receptor for amplification of PIAS is likely to be the same or same type of UVB photoreceptor for induction of anthocyanin synthesis. UVA-amplification of PIAS can be explained by the action of a cryptic red light signal (CRS), an amplification factor for PIAS produced by a distinct phytochrome-species activated by UVA. We suggest that UVA photoreceptors are not involved in anthocyanin synthesis in the broom sorghum.

• Journal of Plant Biology
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• v.19 no.1
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• pp.14-18
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• 1976

Inhibition of flowering in Lemna perpusilla 6746 by 30 mM sucrose was reversed by the addition of acetylcholine (>$10^{-4}M) supplemented with 10^{-4}M$ ascorbic acid to 1/10-strength Hunter's growth medium. The reversible effect of acetylcholine was found to be greater at early stages of flowering than in the later period. Promotive effects of both acetylcholine ($10^{-3}M) and eserine(10^{-5}M$) on flowering in the short-day plant under various photoperiodic conditions were studied. It was indicated that the application decreased length of the critical dark period for the floral induction, and it was also shown that the endogenous status of acetylcholine was involved in the floral response which had a correlation with phytochrome. Interruption of inductive dark periods by red irradiation (1min) immediately followed by far-red light (1 min) completely inhibited flowering, while the addition of acetylcholine and eserine to the medium under the same condition slightly promoted flowering, indicating possible involvement of phytochrome system in acetylcholine activity for photoperiodic sensitivity of floral response in Lemna perpusilla 6746.