• Journal of Photoscience
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• 제7권3호
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• pp.79-86
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• 2000

Phytochromes are red and far-red light absorbing photoreceptors for photomorphogenesis in plants. The red/far wavelength reversible biliproteins are made up of two structural domains. The light-perceiving function of the photoreceptor resides in the N-terminal domain, whereas the signal transducing regulatory function is located within the C-terminal domain. The characteristic role of the phytochromes as phtosensory molecular switches is derived from the phototransformation between two distinct spectral forms, the red light absorbing Pr and the far-red light absorbing Pfr forms. The photoinduced Pr Pfr phototransformation accompanies subtle conformational changes throughout the phytochrome molecule. The conformational signals are subsequently transmitted to the C-terminal domain through various inter-domain crosstalks and induce the interaction of the activated C-terminal domain with phytochrome interacting factors. Thus the inter-domain crosstalks play critical roles in the photoactivation of the phytochromes. Posttranslational modifications, such as the phosphorylation of Ser-598, are also involved in this process through conformational changes and by modulating inter-domain signaling.

• Bulletin of the Korean Chemical Society
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• 제8권4호
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• pp.347-348
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• 1987

• Journal of Microbiology and Biotechnology
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• 제16권9호
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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.

• Applied Biological Chemistry
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• 제32권2호
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• pp.126-131
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• 1989

암소에서 기른 귀리로부터 얻은 59 kD phytochrome의 liposome과 Cibacron Blue dye에 대한 결합성질을 규명하였다. 124 kD 및 118 kD phytochrome과는 달리 Pfr형의 59 kD phytochrome은 liposome 및 Cibacron Blue dye와 정전기적 힘으로 결합한다. 이러한 결과는 124 kD 및 118 kD phytochrome이 Pr형에서 Pfr형으로 광변환시 노출되는 소수표면이 59kD Pfr에는 존재하지 않음을 의미한다. 비교적으로 강한 소수부분이 59 kD polypeptide에 존재함이 알려져 있으므로 C-말단부위로부터 잘려져나간 55 kD tryptic domain이 l18kD 및 124kD Pfr의 소수표면 노출에 중요할 역할을 하는 것으로 믿어진다.

• 한국잡초학회지
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• 제14권3호
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• pp.176-183
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• 1994

새로 합성된 KC6361화합물은 기존 디페닐에 테르계 화합물에서 보였던 증상(회백색)과는 달리 식물체의 백화를 유기시킬 뿐만아니라 암조건에서 녹화를 유기시키는 생리현상을 가지는 바 본 연구에서는 암조건에서 녹화가 유기되었던 원인을 규명하고자 실험하였다. 1. KC6361은 암조건에서 PPIX의 축적, 광전환 후 Pchlide의 재축적 정도, Shibata shift 등에는 영향이 없었던 반면, ALA, Pchl, Chl은 증가되었으며 이중 Pchl의 축적이 현저하였다. 2. KC6361 또는 phytol을 단독처리하거나 KC6361, phytol, ALA 상호간 혼합처리하였을 때 Pchlide의 Pchl로의 전환이 촉진되었던 것으로 보아 KC6361에 의한 암조건에서 녹화는 phytol이 일부 축적되어 이들이 Pchlide와 에스테르화되었기 때문으로 보였다.