scholarly journals PSB33 sustains photosystem II D1 protein under fluctuating light conditions

2017 ◽  
Vol 68 (15) ◽  
pp. 4281-4293 ◽  
Author(s):  
Rikard Fristedt ◽  
Andrea Trotta ◽  
Marjaana Suorsa ◽  
Anders K Nilsson ◽  
Roberta Croce ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
D1 Protein ◽  
Light Conditions ◽  
Fluctuating Light

scholarly journals A chloroplast thylakoid lumen protein is required for proper photosynthetic acclimation of plants under fluctuating light environments

2017 ◽  
Vol 114 (38) ◽  
pp. E8110-E8117 ◽  
Author(s):  
Jun Liu ◽  
Robert L. Last
Keyword(s):  
Photosystem Ii ◽  
Light Stress ◽  
High Irradiance ◽  
Light Conditions ◽  
Agricultural Plant ◽  
Photosynthetic Organisms ◽  
Fluctuating Light ◽  
Stress Susceptibility ◽  
Efficiency And Productivity ◽  
Photosynthetic Adaptation

Despite our increasingly sophisticated understanding of mechanisms ensuring efficient photosynthesis under laboratory-controlled light conditions, less is known about the regulation of photosynthesis under fluctuating light. This is important because—in nature—photosynthetic organisms experience rapid and extreme changes in sunlight, potentially causing deleterious effects on photosynthetic efficiency and productivity. Here we report that the chloroplast thylakoid lumenal protein MAINTENANCE OF PHOTOSYSTEM II UNDER HIGH LIGHT 2 (MPH2; encoded byAt4g02530) is required for growth acclimation ofArabidopsis thalianaplants under controlled photoinhibitory light and fluctuating light environments. Evidence is presented thatmph2mutant light stress susceptibility results from a defect in photosystem II (PSII) repair, and our results are consistent with the hypothesis that MPH2 is involved in disassembling monomeric complexes during regeneration of dimeric functional PSII supercomplexes. Moreover,mph2—and previously characterized PSII repair-defective mutants—exhibited reduced growth under fluctuating light conditions, while PSII photoprotection-impaired mutants did not. These findings suggest that repair is not only required for PSII maintenance under static high-irradiance light conditions but is also a regulatory mechanism facilitating photosynthetic adaptation under fluctuating light environments. This work has implications for improvement of agricultural plant productivity through engineering PSII repair.

scholarly journals The Role of Selected Wavelengths of Light in the Activity of Photosystem II in Gloeobacter violaceus

2021 ◽  
Vol 22 (8) ◽  
pp. 4021
Author(s):  
Monika Kula-Maximenko ◽  
Kamil Jan Zieliński ◽  
Ireneusz Ślesak
Keyword(s):  
Photosystem Ii ◽  
Spectral Composition ◽  
Photosynthetic Electron Transport ◽  
Metabolic Energy ◽  
Light Conditions ◽  
Gloeobacter Violaceus ◽  
Transport Chain ◽  
Cyanobacterial Culture ◽  
Photosynthetic Antennas

Gloeobacter violaceus is a cyanobacteria species with a lack of thylakoids, while photosynthetic antennas, i.e., phycobilisomes (PBSs), photosystem II (PSII), and I (PSI), are located in the cytoplasmic membrane. We verified the hypothesis that blue–red (BR) light supplemented with a far-red (FR), ultraviolet A (UVA), and green (G) light can affect the photosynthetic electron transport chain in PSII and explain the differences in the growth of the G. violaceus culture. The cyanobacteria were cultured under different light conditions. The largest increase in G. violaceus biomass was observed only under BR + FR and BR + G light. Moreover, the shape of the G. violaceus cells was modified by the spectrum with the addition of G light. Furthermore, it was found that both the spectral composition of light and age of the cyanobacterial culture affect the different content of phycobiliproteins in the photosynthetic antennas (PBS). Most likely, in cells grown under light conditions with the addition of FR and G light, the average antenna size increased due to the inactivation of some reaction centers in PSII. Moreover, the role of PSI and gloeorhodopsin as supplementary sources of metabolic energy in the G. violaceus growth is discussed.

Changes in the Stoichiometry of Photosystem II Components as an Adaptive Response to High-Light and Low-Light Conditions during Growth

1986 ◽  
Vol 41 (5-6) ◽  
pp. 597-603 ◽  
Author(s):  
Aloysius Wild ◽  
Matthias Höpfner ◽  
Wolfgang Rühle ◽  
Michael Richter
Keyword(s):  
Photosystem Ii ◽  
Functional Organization ◽  
Photosynthetic Apparatus ◽  
High Light ◽  
Molar Ratio ◽  
Light Conditions ◽  
Low Light ◽  
Pigment System ◽  
Transport Chain ◽  
The One

The effect of different growth light intensities (60 W·m-2, 6 W·m-2) on the performance of the photosynthetic apparatus of mustard plants (Sinapis alba L.) was studied. A distinct decrease in photosystem II content per chlorophyll under low-light conditions compared to high-light conditions was found. For P-680 as well as for Oᴀ and Oв protein the molar ratio between high-light and low-light plants was 1.4 whereas the respective concentrations per chlorophyll showed some variations for P-680 and Oᴀ on the one and Oв protein on the other hand.In addition to the study of photosystem II components, the concentrations of PQ, Cyt f, and P-700 were measured. The light regime during growth had no effect on the amount of P-700 per chlorophyll but there were large differences with respect to PQ and Cyt f. The molar ratio for Cyt f and PQ between high- and low-light leaves was 2.2 and 1.9, respectively.Two models are proposed, showing the functional organization of the pigment system and the electron transport chain in thylakoids of high-light and low-light leaves of mustard plants.

Breakdown of the photosystem II reaction center D1 protein under photoinhibitory conditions: identification and localization of the C-terminal degradation products

Biochemistry ◽  
1991 ◽  
Vol 30 (42) ◽  
pp. 10220-10226 ◽  
Author(s):  
Roberto Barbato ◽  
Giulia Friso ◽  
Maria Teresa Giardi ◽  
Fernanda Rigoni ◽  
Giorgio Mario Giacometti
Keyword(s):  
Photosystem Ii ◽  
Reaction Center ◽  
Degradation Products ◽  
D1 Protein

The Thylakoid FtsH Protease Plays a Role in the Light-Induced Turnover of the Photosystem II D1 Protein

2000 ◽  
Vol 12 (3) ◽  
pp. 419 ◽  
Author(s):  
Marika Lindahl ◽  
Cornelia Spetea ◽  
Torill Hundal ◽  
Amos B. Oppenheim ◽  
Zach Adam ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
D1 Protein ◽  
Ftsh Protease

scholarly journals Evidence that D1 Processing Is Required for Manganese Binding and Extrinsic Protein Assembly into Photosystem II

2004 ◽  
Vol 279 (44) ◽  
pp. 45417-45422 ◽  
Author(s):  
Johnna L. Roose ◽  
Himadri B. Pakrasi
Keyword(s):  
Photosystem Ii ◽  
Mutant Cell ◽  
Protein A ◽  
D1 Protein ◽  
Fluorescence Decay ◽  
Normal Function ◽  
Temporal Position ◽  
Decay Kinetics ◽  
Fluorescence Decay Kinetics ◽  
Extrinsic Proteins

Photosystem II (PSII) is a large membrane protein complex that catalyzes oxidation of water to molecular oxygen. During its normal function, PSII is damaged and frequently turned over. The maturation of the D1 protein, a key component in PSII, is a critical step in PSII biogenesis. The precursor form of D1 (pD1) contains a C-terminal extension, which is removed by the protease CtpA to yield PSII complexes with oxygen evolution activity. To determine the temporal position of D1 processing in the PSII assembly pathway, PSII complexes containing only pD1 were isolated from a CtpA-deficient strain of the cyanobacteriumSynechocystis6803. Although membranes from the mutant cell had nearly 50% manganese, no manganese was detected in isolated ΔctpAHT3 PSII, indicating a severely decreased manganese affinity. However, chlorophyll fluorescence decay kinetics after a single saturating flash suggested that the donor YZwas accessible to exogenous Mn2+ions. Furthermore, the extrinsic proteins PsbO, PsbU, and PsbV were not present in PSII isolated from this mutant. However, PsbO and PsbV were present in mutant membranes, but the amount of PsbV protein was consistently less in the mutant membranes compared with the control membranes. We conclude that D1 processing precedes manganese binding and assembly of the extrinsic proteins into PSII. Interestingly, the Psb27 protein was found to be more abundant in ΔctpAHT3 PSII than in HT3 PSII, suggesting a possible role of Psb27 as an assembly factor during PSII biogenesis.

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