• Journal of Plant Biology
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• 제39권4호
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• pp.301-307
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• 1996

The disassembly of Chl-protein complexes during dark-induced senescence (DIS) was investigated using detached third and fourthleaves of 21$\pm$1 day-old Arabidopsis thaliana. Although Chl content decreased linearly after 1 d, a significant decrease of photochemical effeciency (Fv/Fm) was observed after 2 d. In experiments using native green gel electrophoresis of Chl-protein complexes combined with additional two-dimensional SDS-PAGE analysis, we could observe the degradation of both photosystems after 2 d. Although light-harvesting complex(LHC) for PSI (LHCI) was degraded first in PSI complex, small PSII apoproteins including CP47/CP43 and D1/D2 apoproteins were degraded first in PSII complexes. LHC for PSII (LHCII) trimers were stable until 4 d. The level of LHCII monomers was increased until 3 and decreased thereafter, resulting in the increase of free pigments. These results suggest that the disassembly process of PSI is different from that of PSII.

• Environmental Sciences Bulletin of The Korean Environmental Sciences Society
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• 제3권3호
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• pp.177-188
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• 1999

The effect of ABA on the chloroplast disassembly of Zea mays was investigated by measuring the changes in the relative distribution of chlorophyll(Chl) between the Chl-protein complexes in ABA treated and untreated sensecting leaves. The reaction center(RC)-light harvesting complex(LHC) regions were rapidly disassembled in the late stage of dark-induced senescence. Plus, during dark-induced senescence, the disassembly of a reaction center of P700 apoproteins containing mainly Chl a was faster than that of a reaction center of LHCI apoproteins containing both Chl a and Chl b. The increase in the relative distribution of Chl-protein complexes in the RC-Core2 in the late stage of senescence was due to the accumulation of core complexes such as CP47/43 and reaction centers including D1/D2 apoproteins disassembled from the RC-Corel containing the dimer of D1/D2 apoproteins. The LHCII region was more stable than the other Chl-protein complexes throughout leaf senscence. Accordingly, it is suggested that the preferential breakdown of Chl a gives rise to the disassembly of Chl a-binding proteins, particularly reaction centers and core complexes during dark-induced senescence, plus the primary target of the photosynthetic apparatus in sensecing leaves would seem to be Chl a along with the proteins associated with Chl a. The application of ABA promoted the disassembly of the P700 apoproteins in the PSI reaction center and the dimer of D1/D2 apoproteins, and the conversion of the trimeric LHCII apoprotein to the monometirc LHCII apoprotein during the middle stage of leaf senescence, thereby suggesting that ABA accelerates the disassembly of both Chl a-binding and Chl a+b-binding proteins, particularly Chl a-binding proteins during the middle stage of leaf senescence.

• Journal of Plant Biology
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• 제31권2호
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• pp.131-141
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• 1988

The effects of decursinol and decursin on chloroplast-mediated electron transport and phosphorylation in barley seedlings were investigated in comparison with coumarin in the dark or light. The changes of CP-complexes were also studied. Decursinol, decursin and coumarin caused marked inhibitory effects on germination of seed and electron transport and phosphorylation activity of seedlings. The following order of inhibitory effectiveness was exhibited; decursinol>coumarin>decursin. Loss of chlorophyll and decrease of electron transport activity were retarded in the dark, but were reversely accelerated in the light by these three chemicals. The changes of CP-complex patterns were also similar to effects on chlorophyll content and the electron transport activity. These opposite effect in the dark and light suggest that these three chemicals act as natural growth retardants rather than cytokinins or growth inhibitors.

• Applied Biological Chemistry
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• 제23권1호
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• pp.73-83
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• 1980

디노프라젤레이트(dinoflagellate)들의 광채취색소단백질들은 안데나색소복합체들 내에서 카로테노이드(페리디닌)로부터 크로필 a로 실질적으로 100%의 효율을 갖는 에너지전달현상을 보여준다. 이와같이 디노프라젤레이트에서 광합성을 위한 태양에너지의 채취가 (특히 청(靑)색광에서) 높은 효율로 일어나는 것은 단백질표면의 갈라진 틈안에 위치한 페리디닌과 프로로필 a의 독특한 분자배치에 기인하는 것이다. 고등식물에서 가로테노이드와 크로로필 a 사이에 일어나는 에너지 전달메카니즘에 관해서도 디노프라젤레이트 안데나 색소복합체들과 비교해서 고찰하였다. Algae에서 광합성을 위한 태양에너지, 특히 적(赤)색광의 채취를 다룬 하나의 예로서 Chroomonas Species의 보조광합성색소단백질인 크로오오 모나스 피코시아닌의 분자토포그라피와 에너지전달도 역시 고찰하였다.

• BMB Reports
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• 제29권5호
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• pp.398-404
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• 1996

Light-chilling effects were investigated in chilling-sensitive cucumber (Cucumis sativus L. cv. Ilmichungjang) and chilling-resistant pea (Pisum sativum L. cv. Giant) leaf discs in relation to possible damage in D1 protein. In both plants, dark-chilling did not cause any noticeable changes in (Fv)m/Fm and lincomycin did not affect the decrease in (Fv)m/Fm caused by light-chilling. This result suggests that the de novo synthesis of D1 protein did not occur actively during light-chilling. In pea light-chilled for 6 h. the decreased (Fv)m/Fm was partly recovered in the dark, and almost complete recovery was observed in the light. In cucumber light-chilled for 3 h. the reduced (Fv)m/Fm decreased further for the initial 2 h recovery process in the light regardless of the treatment of lincomycin and recovered very slowly. In both plant species, the treatment of lincomycin inhibited the recovery process in the light, but did not significantly inhibit the process in the dark. In cucumber leaves pulse-labeled with $[^{35}S]Met$, the labeled band intensities of isolated pigment-protein complexes were almost the same during the 6 h light-chilling, but significant decreases in band intensities were observed during the 3 h recovery period. This result suggests that the irreversibly damaged D1 protein was degraded during the recovery period. However, no noticeable changes were observed in the pea leaves during the 12 h chilling and 3 h recovery period. The polyacrylamide gel electrophoresis of the pigment-protein complexes showed that the principal lesion sites of light-chilling were different from those of room temperature photoinhibition.

• Journal of Plant Biology
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• 제29권4호
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• pp.255-262
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• 1986

Developmental changes of chlorophyll-protein (CP)-complex and plastid membrane proteins during the greening of rape (Brassica napus L.) cotyledons were examined in order to investigate the effect of benzymladenine (BA) on plastid development. The formation of CP-complexes was slightly promoted by BA treatment in early greening stage, at 24 h and 48 h after illumination. However, BA inhibited the development of CP-complexes at 72 h after illumination. On the profiles of plastid membrane proteins with greening time, it was found that the 24 kd protein was increased and the 56 kd protein was decreased in both water control and BA-treated cotyledons. However, the above two traits were retarded under BA treatment, respectively. From the obtained result, plastid development of rape cotyledon during greening was partially affected by interaction between light and BA dependent on its physiological age.

• BMB Reports
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• 제34권6호
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• pp.496-501
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• 2001

Lincomycin, an inhibitor of plastid protein synthesis, was found to block the synthesis of apoprotein P700 with a molecular mass of 72 kDa and the assembly of the Chl a-protein of PS I. Synthesis of the polypeptides of 48, 43.5, and 32 kDa of the PS II complex is also suppressed. This process is accompanied by the disappearance of the PS Two reaction center Chl a at 683 nm, and of the PS One reaction center Chl a at 690, 696, and 705 nm on the fourth derivative of the absorption spectra at 77K. Lincomycin does not affect the synthesis of LHC subunits. It increases the content of the two main Chl forms of LHC at 648 nm (Chl b) and 676 nm (Chl a). The low-temperature fluorescence ratio F736/F685 is also increased. However, the effect of cycloheximide (an inhibitor of cytoplasmic protein synthesis) leads to the reduction of polypeptides of the light-harvesting Chl a/b-protein complex in the range of 29.5-22 kDa. Under these conditions, the relative amount of Chl b and the F736/ F685 fluorescence ratio decrease significantly. This is obviously the result of blocking the LHC I and LHC II synthesis. At the same time rifampicin and actinomycin D (inhibitors which block transcription in chloroplast and nuclear genome, respectively) inessentially affect the characteristics of these complexes.

• 한국작물학회:학술대회논문집
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• 한국작물학회 2017년도 9th Asian Crop Science Association conference
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• pp.72-72
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• 2017

We found a new stay-green mutant from 'Pyeongwon' which is an early-maturing rice variety in Korea. The mutant showed green leaves after grain ripening period and it maintained higher SPAD value than wild type rice plant and original variety 'Pyeongwon'. The stay-green trait in rice, three genes have been identified up to date. The non-yellow coloring1 (NYC1) gene encodes a chloroplast-localized short-chain dehydrogenase/reductase (SDR) with three transmembrane domains. The non-yellow coloring3 (NYC3) gene encodes a plastid-localizing alpha/beta hydrolase-fold family protein with an esterase/lipase motif. The Sgr gene encodes a novel chloroplast protein and regulates the destabilization of the light-harvesting chlorophyll binding protein (LHCP) complexes of the thylakoid membranes, which is a prerequisite event for the degradation of chlorophylls and LHCPs during senescence. After sequencing the PCR products, we found a single nucleotide variation($A{\rightarrow}T$) in the NYC1 gene, which changes the amino acid lysine to methionine. The NYC1 gene encodes a short-chain dehydrogenase/reductase(SDR) protein. And we confirmed the co-segregation between SNP and stay-green trait from genotyping the progenies of the mutant.