scholarly journals Inositol polyphosphates and TOR kinase signaling govern photosystem II protein phosphorylation and photosynthetic function under light stress in Chlamydomonas

2021 ◽  
Author(s):  
Inmaculada Couso ◽  
Amanda L. Smythers ◽  
Megan M. Ford ◽  
James G. Umen ◽  
José L. Crespo ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Protein Phosphorylation ◽  
Light Stress ◽  
Kinase Signaling ◽  
Inositol Polyphosphates ◽  
Tor Kinase

scholarly journals Synergism between Inositol Polyphosphates and TOR Kinase Signaling in Nutrient Sensing, Growth Control, and Lipid Metabolism in Chlamydomonas

2016 ◽  
Vol 28 (9) ◽  
pp. 2026-2042 ◽  
Author(s):  
Inmaculada Couso ◽  
Bradley S. Evans ◽  
Jia Li ◽  
Yu Liu ◽  
Fangfang Ma ◽  
...  
Keyword(s):  
Lipid Metabolism ◽  
Growth Control ◽  
Nutrient Sensing ◽  
Kinase Signaling ◽  
Inositol Polyphosphates ◽  
Tor Kinase

Involvement of protein phosphorylation in the sensitivity of photosystem II to strong illumination

1994 ◽  
Vol 92 (1) ◽  
pp. 181-187
Author(s):  
Maria T. Giardi ◽  
Josef Komenda ◽  
Jiri Masojidek
Keyword(s):  
Photosystem Ii ◽  
Protein Phosphorylation

Light stress provokes plastic and elastic modifications in structure and function of photosystem II in camellia leaves

1997 ◽  
Vol 101 (2) ◽  
pp. 265-277 ◽  
Author(s):  
Gert H. J. Kruger ◽  
Merope Tsimilli-Michael ◽  
Reto J. Strasser
Keyword(s):  
Photosystem Ii ◽  
Light Stress ◽  
Structure And Function ◽  
And Function

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.

Protein phosphorylation and magnesium status regulate the degradation of the D1 reaction centre protein of Photosystem II

Plant Science ◽  
1996 ◽  
Vol 115 (2) ◽  
pp. 175-182 ◽  
Author(s):  
Eevi Rintamäki ◽  
Riitta Salo ◽  
Antti Koivuniemi ◽  
Eva-Mari Aro
Keyword(s):  
Photosystem Ii ◽  
Protein Phosphorylation ◽  
Reaction Centre ◽  
Magnesium Status

scholarly journals Evidence for different kinases in thylakoid protein phosphorylation

1987 ◽  
Vol 248 (1) ◽  
pp. 103-108 ◽  
Author(s):  
C H Foyer
Keyword(s):  
Electron Transport ◽  
Protein Kinase ◽  
Photosystem Ii ◽  
Protein Phosphorylation ◽  
System A ◽  
Intact Chloroplasts ◽  
Thylakoid Protein ◽  
Dimethyl Urea ◽  
Thylakoid Protein Phosphorylation ◽  
Differential Action

Thylakoid protein phosphorylation was facilitated in darkness by using the ferredoxin-NADPH system. CoCl2 and DBMIB (2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone) were potent inhibitors of LHCP (light-harvesting chlorophyll-binding protein) phosphorylation, but 3-(3,4-dichlorophenyl)-1,1-dimethyl-urea and atrazine had no significant effect. Differential effects on phosphorylation of the 9 kDa polypeptide and LHCP were observed in darkness with DBMIB and certain other inhibitors specific for Photosystem-II electron transport. Similarly, during illumination of intact chloroplasts or of the reconstituted chloroplast system, a differential action of bicarbonate was observed on the relative phosphorylation of the two proteins. The degree of phosphorylation of the 9 kDa polypeptide was increased in the presence of bicarbonate compared with its absence, whereas that of LHCP was relatively unchanged. Changes in the degree of phosphorylation of the 32 kDa polypeptide in these experiments did not correlate consistently with changes in phosphorylation of either LHCP or the 9 kDa polypeptide, although changes in the 32 kDa polypeptide more often paralleled phosphorylation of the 9 kDa polypeptide rather than the phosphorylation of LHCP. These observations suggest that the protein kinase that phosphorylates LHCP is distinct from that which phosphorylates the 9 kDa polypeptide.

scholarly journals The role of inactive photosystem–II–mediated quenching in a last–ditch community defence against high light stress in vivo

2002 ◽  
Vol 357 (1426) ◽  
pp. 1441-1450 ◽  
Author(s):  
Wah Soon Chow ◽  
Hae–Youn Lee ◽  
Youn–Il Park ◽  
Yong–Mok Park ◽  
Yong–Nam Hong ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Light Stress ◽  
Extreme Environments ◽  
Photosynthetic Apparatus ◽  
Optimal Operation ◽  
Residual Fraction ◽  
Photosynthetic Membrane ◽  
Number Of Factors ◽  
Inactive Photosystem Ii

Photoinactivation of photosystem II (PSII), the light–induced loss of ability to evolve oxygen, is an inevitable event during normal photosynthesis, exacerbated by saturating light but counteracted by repair via new protein synthesis. The photoinactivation of PSII is dependent on the dosage of light: in the absence of repair, typically one PSII is photoinactivated per 10 7 photons, although the exact quantum yield of photoinactivation is modulated by a number of factors, and decreases as fewer active PSII targets are available. PSII complexes initially appear to be photoinactivated independently; however, when less than 30% functional PSII complexes remain, they seem to be protected by strongly dissipative PSII reaction centres in several plant species examined so far, a mechanism which we term ‘inactive PSII–mediated quenching‘. This mechanism appears to require a pH gradient across the photosynthetic membrane for its optimal operation. The residual fraction of functional PSII complexes may, in turn, aid in the recovery of photoinactivated PSII complexes when conditions become less severe. This mechanism may be important for the photosynthetic apparatus in extreme environments such as those experienced by over–wintering evergreen plants, desert plants exposed to drought and full sunlight and shade plants in sustained sunlight.

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