Quality Control of Photosystem II

Yoshioka, Miho; Uchida, Susumu; Mori, Hiroki; Komayama, Keisuke; Ohira, Satoshi; Morita, Noriko; Nakanishi, Tohru; Yamamoto, Yasutake

doi:10.1074/jbc.m602896200

Cited by 119 publications

(51 citation statements)

References 42 publications

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“…9A). However, the heat-induced cleavage of the D1 protein was completely eliminated after the Chelex treatment as reported previously with another chelating agent, EDTA (14), and a strong band representing the D1 aggregation appeared instead (Fig. 9B).…”

Section: Effects Of Heat Stress On the Thylakoids And Ps II Membranesmentioning

confidence: 70%

“…These results suggest that the site of cleavage in the D1 protein during heat stress is the stroma-exposed DE-loop of the D1 protein, being identical to that of the acceptor-side photoinhibition of PS II. In PS II, the moderate heat stress was suggested to destabilize the secondary quinone electron acceptor Q B in the DE-loop of the D1 protein (14), and such a conformational change may be a prerequisite condition for the subsequent cleavage of the D1 protein at the DE-loop.…”

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confidence: 99%

“…It was shown that the treatment of spinach thylakoids at elevated temperatures induced inhibition of oxygen evolution, dephosphorylation of the phos-phoproteins (12,13), cleavage and aggregation of the D1 protein (13,14), and release of three extrinsic proteins PsbO, -P, and -Q from PS II (13,(15)(16)(17). The cleavage products of the D1 protein induced by heat treatment at 40°C for 30 min have a mass of 23 and 9 kDa, which are similar in size to the fragments detected in the acceptor-side photoinhibition of PS II (13,14). These results suggest that the site of cleavage in the D1 protein during heat stress is the stroma-exposed DE-loop of the D1 protein, being identical to that of the acceptor-side photoinhibition of PS II.…”

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confidence: 99%

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Quality Control of Photosystem II

Yamashita

Nijo

Pospı́šil

et al. 2008

Journal of Biological Chemistry

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Moderate heat stress (40°C for 30 min) on spinach thylakoid membranes induced cleavage of the reaction center-binding D1 protein of photosystem II, aggregation of the D1 protein with the neighboring polypeptides D2 and CP43, and release of three extrinsic proteins, PsbO, -P, and -Q. These heat-induced events were suppressed under anaerobic conditions or by the addition of sodium ascorbate, a general scavenger of reactive oxygen species. In accordance with this, singlet oxygen and hydroxyl radicals were detected in spinach photosystem II membranes incubated at 40°C for 30 min with electron paramagnetic resonance spin-trapping spectroscopy. The moderate heat stress also induced significant lipid peroxidation under aerobic conditions. We suggest that the reactive oxygen species are generated by heat-induced inactivation of a water-oxidizing manganese complex and through lipid peroxidation. Although occurring in the dark, the damages caused by the moderate heat stress to photosystem II are quite similar to those induced by excessive illumination where reactive oxygen species are involved. Photosystem II (PS II)3 in higher plants is a multisubunit complex composed of more than 25 proteins and the associated cofactors. Excitation energy captured by the chlorophylls and carotenoids in the light-harvesting chlorophyll protein complexes of PS II is finally transferred to P680, the reaction center chlorophyll of PS II, where charge separation takes place. In particular, PS II performs oxidation of water and reduction of plastoquinone molecules via chlorophyll-mediated photochemical reactions. Although it plays such an important role in the primary photochemical reaction of photosynthesis, PS II is vulnerable to various environmental stresses such as excessive visible light and high temperature.When irradiated with excessive visible light, the D1 protein is oxidatively damaged, and electron transport is inhibited. This process is referred to as photoinhibition of PS II (1-4). The photo-damaged D1 protein is subsequently degraded by specific proteases (5), and the repair of PS II is accomplished by the integration of a newly synthesized D1 protein to the PS II complex (6). Photoinhibition of PS II is caused by either the socalled acceptor-side or donor-side mechanism or both (4, 7). The acceptor-side photoinhibition takes place when the acceptor side of PS II is over-reduced by excessive illumination and the double-reduced Q A molecule is released from its binding site. Reversed electron flow from the primary electron acceptor pheophytin to P680 in the absence of Q A generates the triplet state P680, which reacts with molecular oxygen to form singlet oxygen ( 1 O 2 ). The 1 O 2 eventually damages the nearby polypeptide, the D1 protein. Alternatively, oxygen molecules may be reduced at the acceptor side of PS II to produce superoxide anion radicals (O 2 . ), which are turned into hydrogen peroxide (H 2 O 2 ) and finally hydroxyl radical (HO ⅐ ) through the Fenton reaction (8). It is claimed, however, that the generation of...

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Section: Effects Of Heat Stress On the Thylakoids And Ps II Membranesmentioning

confidence: 70%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Quality Control of Photosystem II

Yamashita

Nijo

Pospı́šil

et al. 2008

Journal of Biological Chemistry

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“…In alkali treated plants, we observed that ATPdependent zinc metalloprotease FTSH 2 (spot 642) was more abundant in S. corniculata. It has been reported that FTSH is the only membrane-bound ATP-dependent protease that functions in the efficient degradation of proteins and is also involved in protection against environmental stress (Yoshioka et al 2006). The up regulation of ATP-dependent zinc metalloprotease FTSH in our study may indicate that it can help to degrade the incorrectly folded proteins, which may be a self-protection mechanism in S. corniculata response to alkali stress.…”

Section: Protein Processing and Amino Acid Metabolismmentioning

confidence: 59%

Integrated proteomics and metabolomics for dissecting the mechanism of global responses to salt and alkali stress in Suaeda corniculata

et al. 2016

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Background and aims Soil alkalinity and salinity are two of the most common environmental stress factors that impact plant growth and productivity. S. corniculata is native to the saline-alkali soil of Northeast China which shows a higher alkali tolerance than other suaeda plants. It will be very important to identify the effect of salt and alkali stress on S. corniculata through proteomics and metabolomics analysis to improve understanding of the resistance of plants. Methods S. corniculata seedlings were exposed to salt and alkali stress for 72 h, respectively. Metabolic changes were quantified by conducting MS-based proteomics and NMR-based metabolomics analysis.Results The response of S. corniculata to salt stress was distinct from that of plants subjected to alkali stress at both physiological and molecular levels. The integrated-omic studies identified 22 and 19 differentially expressed proteins and metabolites mainly involved in carbohydrate metabolism and amino acid metabolism. Conclusions On account of the up-regulation of energy metabolism and higher accumulation of organic osmolytes, S. corniculata shows high pH resistance when it suffers alkali stress. These findings provide insights into the different regulatory mechanisms in halophyte S. corniculata response to salt and alkali stresses.

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“…the photo-or heat-damaged D1 protein in PSII (26,(32)(33)(34)(35)(36)(37)(38). The active form of the FtsH protease has a hexameric ring structure, and its diameter is about 120 Å (39).…”

Section: Discussionmentioning

confidence: 99%

Quality Control of Photosystem II

Khatoon

Inagawa

Pospı́šil

et al. 2009

Journal of Biological Chemistry

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Photosystem II is vulnerable to light damage. The reaction center-binding D1 protein is impaired during excessive illumination and is degraded and removed from photosystem II. Using isolated spinach thylakoids, we investigated the relationship between light-induced unstacking of thylakoids and damage to the D1 protein. Under light stress, thylakoids were expected to become unstacked so that the photodamaged photosystem II complexes in the grana and the proteases could move on the thylakoids for repair. Excessive light induced irreversible unstacking of thylakoids. By comparing the effects of light stress on stacked and unstacked thylakoids, photoinhibition of photosystem II was found to be more prominent in stacked thylakoids than in unstacked thylakoids. In accordance with this finding, EPR spin trapping measurements demonstrated higher production of hydroxyl radicals in stacked thylakoids than in unstacked thylakoids. We propose that unstacking of thylakoids has a crucial role in avoiding further damage to the D1 protein and facilitating degradation of the photodamaged D1 protein under light stress.In the chloroplasts of higher plants and green algae, thylakoid membranes are closely associated and stack to form grana. Under electron microscopy, cylindrical grana consisting of 10 -20 layers of thylakoids have been observed. They have a diameter of 300 -600 nm and are interconnected by lamellae of several hundred nm in length (1, 2). The structure of grana in the chloroplasts of higher plants is well known, but the precise role of grana is incompletely understood. Their possible functions in primary photochemical reactions and subsequent events have been discussed extensively (3-9). Photosystem I (PSI) 3 and II (PSII) complexes are segregated from each other in thylakoids, showing lateral heterogeneity in their distribution. The PSII complex is a multisubunit pigment-protein complex responsible for the photochemical oxidation of water and reduction of plastoquinone (8, 10 -13). It comprises Ͼ25 protein subunits and other low molecular weight cofactors, including chlorophylls, carotenoids, plastoquinones, and manganeses. In the chloroplasts of higher plants, PSII complexes and the associated light-harvesting antenna complex LHCII are not present throughout the thylakoid membranes but are abundant in the grana (2, 14). A densely packed array of PSII complexes in the grana was visualized by electron microscopy (8, 15). Grana formation is more prominent in shade leaves (or shade plants) than in sun leaves (or sun plants), so it has been suggested that enrichment of the PSII⅐LHCII complex in grana is a strategy of plants to collect excitation energy by PSII under weak light (16). The grana structure probably provides an organized environment for PSII. PSI and ATP synthase are located exclusively in the stroma-exposed thylakoids, including the stroma thylakoids, grana end membranes, and grana margins, because these complexes protrude into the stroma. Cytochrome b 6 /f complexes without this protrusion are present unif...

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Quality Control of Photosystem II

Cited by 119 publications

References 42 publications

Quality Control of Photosystem II

Quality Control of Photosystem II

Integrated proteomics and metabolomics for dissecting the mechanism of global responses to salt and alkali stress in Suaeda corniculata

Quality Control of Photosystem II

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