Phosphorylation of PS II polypeptides inhibits D1 protein-degradation and increases PS II stability

1996 ◽  
Vol 50 (3) ◽  
pp. 257-269 ◽  
Author(s):  
Volker Ebbert ◽  
Doris Godde
Keyword(s):  
Protein Degradation ◽  
D1 Protein ◽  
Ps Ii

Differential Sensitivity of 32 kDa-D1 Protein Degradation and Photosynthetic Electron Flow to Photosystem II Herbicides

1990 ◽  
Vol 45 (5) ◽  
pp. 408-411 ◽  
Author(s):  
Marcel A. K. Jansen ◽  
Shmuel Malkin ◽  
Marvin Edelman
Keyword(s):  
Photosystem Ii ◽  
Visible Light ◽  
Protein Degradation ◽  
Electron Flow ◽  
Protein A ◽  
D1 Protein ◽  
Differential Sensitivity ◽  
Reaction Centre ◽  
Ps Ii ◽  
Specific Effects

Abstract Degradation of the 32 kDa-D1 protein, a photosystem II reaction centre component, was studied as a function of linear electron flow in visible light in the presence of various photosys­ tem II herbicides. Under these conditions, herbicide specific effects on protein degradation were clearly evident. 32 kDa-D 1 protein degradation and electron flow between Qa and Qb proved to be only partially correlated. We conclude that inhibition of protein degradation by PS II herbicides in visible light is not simply correlated to displacement of Qb.

Degradation of unassembled and damaged thylakoid proteins

2001 ◽  
Vol 29 (4) ◽  
pp. 427-430 ◽  
Author(s):  
Z. Adam ◽  
O. Ostersetzer
Keyword(s):  
Thylakoid Membrane ◽  
D1 Protein ◽  
Thylakoid Membranes ◽  
Reaction Centre ◽  
Ps Ii ◽  
Plant Genomes ◽  
Thylakoid Membrane Proteins ◽  
Luminal Side ◽  
Cytochrome Complex ◽  
Aaa Protein

To study protein degradation in thylakoid membranes we identified, characterized and cloned thylakoid proteases, and then linked them to known proteolytic processes. Several families of chloroplast proteases were identified and characterized to different extents. FtsH, an ATP-dependent metalloprotease that belongs to the AAA-protein family, was found to be integral to the thylakoid membrane, facing the stroma. It is involved in both the degradation of unassembled subunits of membrane complexes, such as the Rieske Fe-S protein of the cytochrome complex, and the degradation of oxidatively damaged proteins such as the D1 protein of the photosystem II (PS II) reaction centre. Plant genomes contain multiple isomers of this protease but the functional significance of this multiplication is not clear yet. A second protease, the serine ATP-independent DegP, was found to be strongly associated with the luminal side of the thylakoid membrane. Although a specific role has not yet assigned for it, its location suggests that it can degrade luminal soluble proteins as well as luminally exposed regions of thylakoid membrane proteins.

D1 protein turnover and carotene synthesis in relation to zeaxanthin epoxidation in rice leaves during recovery from low temperature photoinhibition

2000 ◽  
Vol 27 (3) ◽  
pp. 239 ◽  
Author(s):  
Chang-Cheng Xu ◽  
Tingyun Kuang ◽  
Liangbi Li ◽  
Choon-Hwan Lee
Keyword(s):  
Protein Turnover ◽  
Oryza Sativa L ◽  
D1 Protein ◽  
Inhibitory Effect ◽  
High Light ◽  
Slow Increase ◽  
Ps Ii ◽  
Rice Leaves ◽  
The Relationship ◽  
Carotene Synthesis

The relationship between D1 protein turnover, carotene synthesis and zeaxanthin epoxidation was exam-ined in rice (Oryza sativa L.) leaves during recovery subsequent to chilling treatments at 500 (moderate light) or 1000 mol photons m –2 s –1 (high light) for 3 h. When recovery was monitored in the light, the decrease in the level of zeaxanthin was closely paralleled by the slow increase in the efficiency of photosystem (PS) II. Both these processes were greatly slowed down in the presence of lincomycin, an inhibitor of chloroplast-coded protein synthesis. In leaves chilled in moderate light, the inhibitory effect of lincomycin on zeaxanthin decrease was largely eliminated by infiltration with dithiothreitol, an inhibitor of de-epoxidase, suggesting a stimulation of violaxanthin de-epoxidation rather than an inhibition of zeaxanthin epoxidation in the presence of lincomycin. In high-light-chilled leaves, lincomycin had little impact on violaxanthin de-epoxidation but strikingly blocked the process of zeaxanthin epoxidation. Furthermore both PSII recovery and zeaxanthin epoxidation in high-light-chilled leaves were almost completely suppressed by incubation with either fluridone or norflurazon, two inhibitors of carotene synthesis. The possible reason for parallel changes in the level of zeaxanthin and PSII efficiency during recovery from photoinhibition is discussed.

Chitooligosaccharides enhance cold tolerance by repairing photodamaged PS II in rice

2018 ◽  
Vol 156 (7) ◽  
pp. 888-899 ◽  
Author(s):  
Jiachun Zhou ◽  
Qiao Chen ◽  
Yang Zhang ◽  
Liqiang Fan ◽  
Zhen Qin ◽  
...  
Keyword(s):  
Cold Stress ◽  
Cold Resistance ◽  
D1 Protein ◽  
Pcr Analysis ◽  
Dependent Manner ◽  
Osmotic Regulation ◽  
Ps Ii ◽  
Protein Encoding ◽  
Polymerase Chain ◽  
Oxidation Damage

AbstractChitooligosaccharides (COS) are multi-functional foods and nutrients and environmentally friendly biological abiotic-resistance inducing agents for plants. In the current study, the effects and possible mechanisms of COS on improving the cold resistance of rice (II YOU 1259) seedlings were investigated. Compared with the control, a COS pre-soaking treatment enhanced photosynthesis, reduced oxidation damage and led to accumulation of more osmotic regulation substances under chilling treatment. In addition, a novel Deg/HtrA family serine endopeptidase (DegQ) gene, related to COS enhanced rice cold resistance, was identified. Quantitative real-time polymerase chain reaction (qRT-PCR) analysis revealed that transcription of DegQ and psbA (D1 protein encoding gene) were up-regulated in a time-dependent manner by COS treatment under cold stress. With increasing expression of the D1 protein, chlorophyll b content was enhanced correspondingly. The current results suggest that COS could enhance cold stress tolerance of rice by repairing the photodamaged photosystem II, altering osmotic regulation and reducing oxidation damage.

In vitro studies on light-induced inhibition of Photosystem II and D1-protein degradation at low temperatures

1990 ◽  
Vol 1019 (3) ◽  
pp. 269-275 ◽  
Author(s):  
Eva-Mari Aro ◽  
Torill Hundal ◽  
Inger Carlberg ◽  
Bertil Andersson
Keyword(s):  
Photosystem Ii ◽  
Protein Degradation ◽  
Low Temperatures ◽  
D1 Protein ◽  
In Vitro Studies
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