Recovery of photosynthesis and photosystem II fluorescence in Chlamydomonas reinhardtii after exposure to three levels of high light

1992 ◽  
Vol 85 (1) ◽  
pp. 61-68 ◽  
Author(s):  
Stefan Falk ◽  
Goran Samuelsson
2009 ◽  
Vol 8 (11) ◽  
pp. 1648-1657 ◽  
Author(s):  
Anchalee Sirikhachornkit ◽  
Jai W. Shin ◽  
Irene Baroli ◽  
Krishna K. Niyogi

ABSTRACT Tocopherols (vitamin E) comprise a class of lipid-soluble antioxidants synthesized only in plants, algae, and some cyanobacteria. The majority of tocopherols in photosynthetic cells is in the α form, which has the highest vitamin E activity in humans, whereas the β, γ, and δ forms normally account for a small percentage of total tocopherols. The antioxidant activities of these forms of tocopherol differ depending on the experimental system, and their relative activities in vivo are unclear. In a screen for suppressors of the xanthophyll-deficient npq1 lor1 double mutant of Chlamydomonas reinhardtii, we isolated a vte3 mutant lacking α-tocopherol but instead accumulating β-tocopherol. The vte3 mutant contains a mutation in the homolog of a 2-methyl-6-phytyl-1,4-benzoquinone methyltransferase gene found in plants. The vte3 npq1 lor1 triple mutant with β-tocopherol survived better under photooxidative stress than did the npq1 lor1 mutant, but the vte3 mutant on its own did not have an obvious phenotype. Following transfer from low light to high light, the triple mutant showed a higher efficiency of photosystem II, a higher level of cell viability, and a lower level of lipid peroxide, a marker for oxidative stress, than did the npq1 lor1 mutant. After high-light transfer, the level of the photosystem II reaction center protein, D1, was also higher in the vte3 npq1 lor1 mutant, but the rate of D1 photodamage was not significantly different from that of the npq1 lor1 mutant. Taken together, these results suggest that the replacement of α-tocopherol by β-tocopherol in a xanthophyll-deficient strain of Chlamydomonas reinhardtii contributes to better survival under conditions of photooxidative stress.


2016 ◽  
Vol 291 (33) ◽  
pp. 17478-17487 ◽  
Author(s):  
Viviana Correa-Galvis ◽  
Petra Redekop ◽  
Katharine Guan ◽  
Annika Griess ◽  
Thuy B. Truong ◽  
...  

Non-photochemical quenching of excess excitation energy is an important photoprotective mechanism in photosynthetic organisms. In Arabidopsis thaliana, a high quenching capacity is constitutively present and depends on the PsbS protein. In the green alga Chlamydomonas reinhardtii, non-photochemical quenching becomes activated upon high light acclimation and requires the accumulation of light harvesting complex stress-related (LHCSR) proteins. Expression of the PsbS protein in C. reinhardtii has not been reported yet. Here, we show that PsbS is a light-induced protein in C. reinhardtii, whose accumulation under high light is further controlled by CO2 availability. PsbS accumulated after several hours of high light illumination at low CO2. At high CO2, however, PsbS was only transiently expressed under high light and was degraded after 1 h of high light exposure. PsbS accumulation correlated with an enhanced non-photochemical quenching capacity in high light-acclimated cells grown at low CO2. However, PsbS could not compensate for the function of LHCSR in an LHCSR-deficient mutant. Knockdown of PsbS accumulation led to reduction of both non-photochemical quenching capacity and LHCSR3 accumulation. Our data suggest that PsbS is essential for the activation of non-photochemical quenching in C. reinhardtii, possibly by promoting conformational changes required for activation of LHCSR3-dependent quenching in the antenna of photosystem II.


2020 ◽  
Author(s):  
Marie Chazaux ◽  
Stefano Caffarri ◽  
Juliane Da Graça ◽  
Stephan Cuiné ◽  
Magali Floriani ◽  
...  

AbstractPhotosynthetic organisms require acclimation mechanisms to regulate photosynthesis in response to light conditions. Here, two mutant alleles of ACCLIMATION OF PHOTOSYNTHESIS TO THE ENVIRONMENT 1 (ape1) have been characterized in Chlamydomonas reinhardtii. The ape1 mutants are photosensitive and show PSII photoinhibition during high light acclimation or under high light stress. The ape1 mutants retain more PSII super-complexes and have changes to thylakoid stacking relative to control strains during photosynthetic growth at different light intensities. The APE1 protein is found in all oxygenic phototrophs and encodes a 25 kDa thylakoid protein that interacts with the Photosystem II core complex as monomers, dimers and supercomplexes. We propose a model where APE1 bound to PSII supercomplexes releases core complexes and promotes PSII heterogeneity influencing the stacking of Chlamydomonas thylakoids. APE1 is a regulator in light acclimation and its function is to reduce over-excitation of PSII centres and avoid PSII photoinhibition to increase the resilience of photosynthesis to high light.


2018 ◽  
Vol 115 (14) ◽  
pp. 3722-3727 ◽  
Author(s):  
Kotaro Kosuge ◽  
Ryutaro Tokutsu ◽  
Eunchul Kim ◽  
Seiji Akimoto ◽  
Makio Yokono ◽  
...  

Photosynthetic organisms are frequently exposed to light intensities that surpass the photosynthetic electron transport capacity. Under these conditions, the excess absorbed energy can be transferred from excited chlorophyll in the triplet state (3Chl*) to molecular O2, which leads to the production of harmful reactive oxygen species. To avoid this photooxidative stress, photosynthetic organisms must respond to excess light. In the green alga Chlamydomonas reinhardtii, the fastest response to high light is nonphotochemical quenching, a process that allows safe dissipation of the excess energy as heat. The two proteins, UV-inducible LHCSR1 and blue light-inducible LHCSR3, appear to be responsible for this function. While the LHCSR3 protein has been intensively studied, the role of LHCSR1 has been only partially elucidated. To investigate the molecular functions of LHCSR1 in C. reinhardtii, we performed biochemical and spectroscopic experiments and found that the protein mediates excitation energy transfer from light-harvesting complexes for Photosystem II (LHCII) to Photosystem I (PSI), rather than Photosystem II, at a low pH. This altered excitation transfer allows remarkable fluorescence quenching under high light. Our findings suggest that there is a PSI-dependent photoprotection mechanism that is facilitated by LHCSR1.


1986 ◽  
Vol 41 (5-6) ◽  
pp. 597-603 ◽  
Author(s):  
Aloysius Wild ◽  
Matthias Höpfner ◽  
Wolfgang Rühle ◽  
Michael Richter

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.


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