Psb30 is a photosystem II reaction center subunit and is required for optimal growth in high light in Chlamydomonas reinhardtii

2011 ◽  
Vol 104 (1-2) ◽  
pp. 220-228 ◽  
Author(s):  
Natsuko Inoue-Kashino ◽  
Yasuhiro Kashino ◽  
Yuichiro Takahashi
2007 ◽  
Vol 85 (6) ◽  
pp. 721-729 ◽  
Author(s):  
Tessa Pocock ◽  
P. V. Sane ◽  
S. Falk ◽  
N. P.A. Hüner

Using in vivo thermoluminescence, we examined the effects of growth irradiance and growth temperature on charge recombination events in photosystem II reaction centres of the model green alga Chlamydomonas reinhardtii. We report that growth at increasing irradiance at either 29 or 15 °C resulted in comparable downward shifts in the temperature peak maxima (TM) for S2QB– charge pair recombination events, with minimal changes in S2QA– recombination events. This indicates that such growth conditions decrease the activation energy required for S2QB– charge pair recombination events with no concomitant change in the activation energy for S2QA– recombination events. This resulted in a decrease in the ΔTM between S2QA– and S2QB– recombination events, which was reversible when shifting cells from low to high irradiance and back to low irradiance at 29 °C. We interpret these results to indicate that the redox potential of QB was modulated independently of QA, which consequently narrowed the redox potential gap between QA and QB in photosystem II reaction centres. Since a decrease in the ΔTM between S2QA– and S2QB– recombination events correlated with growth at increasing excitation pressure, we conclude that acclimation to growth under high excitation pressure narrows the redox potential gap between QA and QB in photosystem II reaction centres, enhancing the probability for reaction center quenching in C. reinhardtii. We discuss the molecular basis for the modulation of the redox state of QB, and suggest that the potential for reaction center quenching complements antenna quenching via the xanthophyll cycle in the photoprotection of C. reinhardtii from excess light.


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.


2012 ◽  
Vol 116 (16) ◽  
pp. 4860-4870 ◽  
Author(s):  
Khem Acharya ◽  
Valter Zazubovich ◽  
Mike Reppert ◽  
Ryszard Jankowiak

1990 ◽  
Vol 45 (5) ◽  
pp. 395-401 ◽  
Author(s):  
Susana Shochat ◽  
Noam Adir ◽  
Alma Gal ◽  
Yorinao Inoue ◽  
Laurence Mets ◽  
...  

Abstract The effect of unoccupancy of the QB site by plastoquinone on the photoinactivation of reaction center II in a Cyt b6/f-less mutant of Chlamydomonas reinhardtii, B6, was investigated. In these cells the oxidation of plastoquinol generated by electron flow via RC II to plastoquinone and thus the turnover of PQH2/PQ via the QB site are drastically reduced. Reaction center II of the mutant cells was resistant to photoinactivation relative to the control cells as demonstrated by measurements of light-induced destabilization of S2-QB charge recombination, rise in in­ trinsic fluorescence and loss of variable fluorescence. These parameters relate to functions in­ volving the reaction center II D1 protein. The light-induced degradation of D1 in the mutant cells was also considerably reduced, with a t 1/2 value of 7 h as compared, under similar conditions, to about 1.5 h for the control cells. These results indicate that the photoinactivation of RC II and turnover of the D1 protein are related and require occupancy of the QB site by PQ and its light-driven reduction.


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.


Sign in / Sign up

Export Citation Format

Share Document