Quality control of Photosystem II: Cleavage and aggregation of heat-damaged D1 protein in spinach thylakoids

Komayama, Keisuke; Khatoon, Mahbuba; Takenaka, Daichi; Horie, Junko; Yamashita, Amu; Yoshioka, Miho; Nakayama, Yohsuke; Yoshida, Mari; Ohira, Satoshi; Morita, Noriko; Velitchkova, Maya; Enami, Isao; Yamamoto, Yasutake

doi:10.1016/j.bbabio.2007.05.001

Cited by 65 publications

(64 citation statements)

References 44 publications

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“…1A), cleavage of the D1 protein was monitored by Western blot analysis with specific antibodies against the D1-DE loop and the C-terminal part of the D1 protein. Two fragments of the D1 protein, a 23-kDa N-terminal fragment and a 9-kDa C-terminal fragment, were detected under aerobic conditions, as reported previously (13) (Fig. 1B).…”

Section: Heat-induced Cleavage and Aggregation Of The D1 Protein In Ssupporting

confidence: 88%

“…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: Heat-induced Cleavage and Aggregation Of The D1 Protein In Ssupporting

confidence: 88%

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confidence: 99%

Quality Control of Photosystem II

Yamashita

Nijo

Pospı́šil

et al. 2008

Journal of Biological Chemistry

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“…In this proteolysis, it was demonstrated that the substrate D1 protein is degraded from the N-terminus. However, such a "processive" degradation of the D1 protein does not apply apparently in the degradation of the damaged D1 protein in higher plant chloroplasts under high light or high temperatures [29,30,39].…”

Section: Specific Roles Of Ftsh Proteases In the Cyanobacteria And Chmentioning

confidence: 99%

“…Similar damage and degradation processes of the D1 protein were also seen under moderate heat stress when spinach thylakoids were incubated at 40 °C for 30 min in the dark (hereafter heat-inactivation of PSII) [29,30]. In both photoinhibition and heat-inactivation, the protease systems work for swift repair of PSII in the thylakoid membrane, and also possibly in the stroma and in the thylakoid lumen [6].…”

Section: Introductionmentioning

confidence: 97%

Quality control of Photosystem II: The molecular basis for the action of FtsH protease and the dynamics of the thylakoid membranes

Yoshioka-Nishimura

Yamamoto

2014

Journal of Photochemistry and Photobiology B: Biology

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The reaction center-binding D1 protein of Photosystem II is damaged by excessive light, which leads to photoinhibition of Photosystem II. The damaged D1 protein is removed immediately by specific proteases, and a metalloprotease FtsH located in the thylakoid membranes is involved in the proteolytic process. According to recent studies on the distribution and organization of the protein complexes/supercomplexes in the thylakoid membranes, the grana of higher plant chloroplasts are crowded with Photosystem II complexes and light-harvesting complexes. For the repair of the photodamaged D1 protein, the majority of the active hexameric FtsH proteases should be localized in close proximity to the Photosystem II complexes. The unstacking of the grana may increase the area of the grana margin and facilitate easier access of the FtsH proteases to the damaged D1 protein. These results suggest that the structural changes of the thylakoid membranes by light stress increase the mobility of the membrane proteins and support the quality control of Photosystem II. (159 words)

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“…Photosystem II (PSII) is extremely sensitive to Cd, and its func- (Mallick and Mohn, 2003). In addition, damages to PSII are mostly localized at the D1 protein (Pagliano et al, 2006;Komayama et al, 2007;Murata et al, 2007). However, little is known about the metabolic changes of the major functional proteins and the corresponding transcripts of PSII as well as the changes of the alternative respiratory pathway in mitochondria with cadmium stress, especially in different plant cultivars.…”

Section: Introductionmentioning

confidence: 99%

Effects of Cadmium Stress on Alternative Oxidase and Photosystem II in Three Wheat Cultivars

Duan

Yuan

et al. 2010

Zeitschrift Für Naturforschung C

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The effects of Cd stress (200 μmol/L, 8 days) on respiration and photosynthesis of three wheat cultivars were investigated: Chuanyu 12 (CY12), Chuanmai 42 (CM42), and Chuanmai 47 (CM47). Fifteen-day-old seedlings were exposed to 200 μmol/L CdCl 2 for 4 days and 8 days, respectively. The results indicated that Cd was accumulated largely in roots, but little in leaves of all three cultivars. CY12 accumulated the highest level of Cd in roots and showed the weakest resistance. On the contrary, the other two cultivars, CM42 and CM47, adapted better to Cd stress, and their thiobarbituric acid-reactive substances (TBARS) contents were lower than in CY12, but the chlorophyll contents and water contents were higher than in CY12. Additionally, Cd stress prompted the alternative oxidase (AOX) activity and upregulated the cyanide-resistant respiration in CM42 and CM47 after 8 days; no such induction was observed for CY12. The CO 2 assimilation rate, leaf stomatal conductance and chlorophyll fl uorescence were inhibited by Cd stress in all cultivars, but more severe in the CY12 cultivar. Western blots indicated that the content of the photosystem II proteins LHCII and D1 decreased in CY12, but did not change in CM42 and CM47. While the content of the mitochondrial AOX protein increased markedly in CM42 and CM47, it did not in CY12. These results suggested that AOX and LHCII could be regarded as indicators of plant's resistance to heavy metals.

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Quality control of Photosystem II: Cleavage and aggregation of heat-damaged D1 protein in spinach thylakoids

Cited by 65 publications

References 44 publications

Quality Control of Photosystem II

Quality Control of Photosystem II

Quality control of Photosystem II: The molecular basis for the action of FtsH protease and the dynamics of the thylakoid membranes

Effects of Cadmium Stress on Alternative Oxidase and Photosystem II in Three Wheat Cultivars

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