The light-harvesting chlorophyll a/b-protein complex of photosystem II (LHCII) is the most abundant membrane protein in green plants, and its degradation is a crucial process for the acclimation to high light conditions and for the recovery of nitrogen (N) and carbon (C) during senescence. However, the molecular mechanism of LHCII degradation is largely unknown. Here, we report that chlorophyll b reductase, which catalyzes the first step of chlorophyll b degradation, plays a central role in LHCII degradation. When the genes for chlorophyll b reductases NOL and NYC1 were disrupted in Arabidopsis thaliana, chlorophyll b and LHCII were not degraded during senescence, whereas other pigment complexes completely disappeared. When purified trimeric LHCII was incubated with recombinant chlorophyll b reductase (NOL), expressed in Escherichia coli, the chlorophyll b in LHCII was converted to 7-hydroxymethyl chlorophyll a. Accompanying this conversion, chlorophylls were released from LHCII apoproteins until all the chlorophyll molecules in LHCII dissociated from the complexes. Chlorophyll-depleted LHCII apoproteins did not dissociate into monomeric forms but remained in the trimeric form. Based on these results, we propose the novel hypothesis that chlorophyll b reductase catalyzes the initial step of LHCII degradation, and that trimeric LHCII is a substrate of LHCII degradation.Photosynthesis is an indispensable process for plants to generate chemical energy for biological processes. Chlorophyll plays a central role in photosynthesis by harvesting light energy (1) and driving electron transfer (2). Chlorophyll exists as chlorophyll-protein complexes, which can be divided into two groups (3). One group consists of the core antenna complexes, which include CP43/CP47 of photosystem (PS) 2 II and P700-chlorophyll a-protein complexes of PSI (CP1). The composition and organization of these core antenna complexes is conserved in oxygenic phototrophs. The second group consists of peripheral antenna complexes, which harvest and transfer light energy to the core antenna complexes. Land plants and green algae contain light-harvesting complex II (LHCII) as a peripheral antenna complex (4, 5). LHCII is the most abundant pigment-protein complex, binding chlorophyll a and b, which account for Ͼ40% of the total chlorophyll (6, 7). In addition to its light-harvesting function, LHCII regulates energy distribution between PSI and PSII (6), and is involved in the dissipation of excess light energy (8). It is known that the amount of LHCII varies depending on developmental stages and changes in light environments (9). Taken together, it is considered that the formation and degradation of LHCII are important processes for the survival of plants (10).LHCII formation has been extensively studied using mutants and transgenic plants of various species. These studies have clarified the close relationship between chlorophyll synthesis and the LHCII formation. LHCII does not accumulate in chlorophyll b-less mutants, probably because LHCII is not stab...

Mixture of brown rice and rice bran fermented with Aspergillus oryzae, designated as FBRA, has been reported to reveal anti-carcinogenic and anti-inflammatory effects in rodents. Then, to test its potential anti-cancer activity, the aqueous extract was prepared from FBRA powder, and the effect of this extract on human acute lymphoblastic leukemia Jurkat cells was directly examined. The exposure to FBRA extract reduced the cell viability in a concentration- and time-dependent manner. The reduction of the cell viability was accompanied by the DNA fragmentation, and partially restored by treatment with pan-caspase inhibitor. Further studies showed that FBRA extract induced the cleavage of caspase-8, -9, and -3, and decreased Bcl-2 protein expression. Moreover, the expression of tBid, DR5, and Fas proteins was enhanced by FBRA extract, and the pretreatment with caspase-8 inhibitor, but not caspase-9 inhibitor, restored the reduction of the cell viability induced by FBRA extract. These findings suggested that FBRA extract could induce the apoptotic death of human acute lymphoblastic leukemia cells probably through mainly the death receptor-mediated pathway and supplementarily through the tBid-mediated mitochondrial pathway, proposing the possibility that FBRA was a potential functional food beneficial to patients with hematological cancer.

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Many studies have demonstrated that the dietary supplementation of polyamines, especially spermidine (SPD), prevents age-related diseases. Rice bran is rich in polyamines and their amounts could be increased by fermentation with Aspergillus oryzae (A. oryzae). In this study, we developed a method for the determination of putrescine (PUT), SPD and spermine (SPM) in rice bran samples by liquid chromatography/electrospray ionization-tandem mass spectrometry (LC/ESI-MS/MS) after derivatization with 4-(N,N-dimethylaminosulfonyl)-7-fluoro-2,1,3-benzoxadiazole (DBD-F). The derivatization improved the LC retention and ESI-MS/MS detectability of the polyamines, and consequently enabled precise and accurate quantification. Using this method, we found that the SPD content increased to 158% due to fermentation with A. oryzae, while the content of PUT and SPM decreased. SPD is known as the polyamine playing a central role in cell proliferation and growth, and therefore has health benefits. The fermented rice bran might be a good material for functional foods aimed at SPD supplementation.