scholarly journals The Chlamydomonas reinhardtii cia3 Mutant Lacking a Thylakoid Lumen-Localized Carbonic Anhydrase Is Limited by CO2 Supply to Rubisco and Not Photosystem II Function in Vivo

2003 ◽  
Vol 132 (4) ◽  
pp. 2267-2275 ◽  
Author(s):  
David Thomas Hanson ◽  
Linda A. Franklin ◽  
Goran Samuelsson ◽  
Murray R. Badger
Keyword(s):  
Photosystem Ii ◽  
Carbonic Anhydrase ◽  
Chlamydomonas Reinhardtii ◽  
Thylakoid Lumen

scholarly journals Thylakoid Lumen Carbonic Anhydrase (CAH3) Mutation Suppresses Air-Dier Phenotype of LCIB Mutant in Chlamydomonas reinhardtii

2008 ◽  
Vol 149 (2) ◽  
pp. 929-937 ◽  
Author(s):  
Deqiang Duanmu ◽  
Yingjun Wang ◽  
Martin H. Spalding
Keyword(s):  
Carbonic Anhydrase ◽  
Chlamydomonas Reinhardtii ◽  
Thylakoid Lumen

Excitation pressure regulates the activation energy for recombination events in the photosystem II reaction centres of Chlamydomonas reinhardtii

2007 ◽  
Vol 85 (6) ◽  
pp. 721-729 ◽  
Author(s):  
Tessa Pocock ◽  
P. V. Sane ◽  
S. Falk ◽  
N. P.A. Hüner
Keyword(s):  
Activation Energy ◽  
Photosystem Ii ◽  
Redox Potential ◽  
Chlamydomonas Reinhardtii ◽  
Reaction Center ◽  
Growth Conditions ◽  
High Irradiance ◽  
Reaction Centres ◽  
Excitation Pressure

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.

The carbonic anhydrase gene families of Chlamydomonas reinhardtii

2005 ◽  
Vol 83 (7) ◽  
pp. 780-795 ◽  
Author(s):  
Mautusi Mitra ◽  
Catherine B Mason ◽  
Ying Xiao ◽  
Ruby A Ynalvez ◽  
Scott M Lato ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Chlamydomonas Reinhardtii ◽  
Gene Families ◽  
Carbonic Anhydrases ◽  
Photosynthetic Organisms ◽  
Surrounding Environment ◽  
Concentrating Mechanism ◽  
Chloroplast Stroma ◽  
Carbonic Anhydrase Gene

Carbonic anhydrases (CAs) are zinc-containing metalloenzymes that catalyze the reversible interconversion of CO2 and HCO3–. Aquatic photosynthetic organisms have evolved different forms of CO2-concentrating mechanisms to aid Rubisco in capturing CO2 from the surrounding environment. One aspect of all CO2-concentrating mechanisms is the critical roles played by various specially localized extracellular and intracellular CAs. There are three evolutionarily unrelated CA families designated α-, β-, and γ-CA. In the green alga, Chlamydomonas reinhardtii Dangeard, eight CAs have now been identified, including three α-CAs and five β-CAs. In addition, C. reinhardtii has another CA-like gene, Glp1 that is similar to known γ-CAs. To characterize these different CA isoforms, some of the CA genes have been overexpressed to determine whether the proteins have CA activity and to generate antibodies for in vivo immunolocalization. The CA proteins Cah3, Cah6, and Cah8, and the γ-CA-like protein, Glp1, have been overexpressed. Cah3, Cah6, and Cah8 have CA activity, but Glp1 does not. At least two of these proteins, Cah3 and Cah6, are localized to the chloroplast. Using immunolocalization and sequence analyses, we have determined that Cah6 is located to the chloroplast stroma and confirmed that Cah3 is localized to the chloroplast thylakoid lumen. Activity assays show that Cah3 is 100 times more sensitive to sulfonamides than Cah6. We present a model on how these two chloroplast CAs might participate in the CO2-concentrating mechanism of C. reinhardtii. Key words: carbonic anhydrase, CO2-concentrating mechanism, Chlamydomonas, immunolocalization.

scholarly journals Role of a novel photosystem II-associated carbonic anhydrase in photosynthetic carbon assimilation in Chlamydomonas reinhardtii

FEBS Letters ◽  
1999 ◽  
Vol 444 (1) ◽  
pp. 102-105 ◽  
Author(s):  
Youn-Il Park ◽  
Jan Karlsson ◽  
Igor Rojdestvenski ◽  
Natalia Pronina ◽  
Viacheslav Klimov ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Carbonic Anhydrase ◽  
Chlamydomonas Reinhardtii ◽  
Carbon Assimilation ◽  
Photosynthetic Carbon ◽  
Photosynthetic Carbon Assimilation

scholarly journals Replacement of α-Tocopherol by β-Tocopherol Enhances Resistance to Photooxidative Stress in a Xanthophyll-Deficient Strain of Chlamydomonas reinhardtii

2009 ◽  
Vol 8 (11) ◽  
pp. 1648-1657 ◽  
Author(s):  
Anchalee Sirikhachornkit ◽  
Jai W. Shin ◽  
Irene Baroli ◽  
Krishna K. Niyogi
Keyword(s):  
Vitamin E ◽  
Photosystem Ii ◽  
Chlamydomonas Reinhardtii ◽  
Antioxidant Activities ◽  
Lipid Peroxide ◽  
Experimental System ◽  
High Light ◽  
Photooxidative Stress ◽  
Triple Mutant

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.

scholarly journals Correlation between changes in light energy distribution and changes in thylakoid membrane polypeptide phosphorylation in Chlamydomonas reinhardtii.

1984 ◽  
Vol 98 (1) ◽  
pp. 1-7 ◽  
Author(s):  
F A Wollman ◽  
P Delepelaire
Keyword(s):  
Photosystem Ii ◽  
Chlamydomonas Reinhardtii ◽  
Redox State ◽  
Light Harvesting ◽  
Anaerobic Treatment ◽  
Intact Cells ◽  
Light Harvesting Complex ◽  
Plastoquinone Pool

We have used a new method to extensively modify the redox state of the plastoquinone pool in Chlamydomonas reinhardtii intact cells. This was achieved by an anaerobic treatment that inhibits the chlororespiratory pathway recently described by P. Bennoun (Proc. Natl. Acad. Sci. USA, 1982, 79:4352-4356). A state I (plus 3,4-dichlorophenyl-1,1-dimethylurea) leads to anaerobic state transition induced a decrease in the maximal fluorescence yield at room temperature and in the FPSII/FPSI ratio at 77 degrees K, which was three times larger than in a classical state I leads to state II transition. The fluorescence changes observed in vivo were similar in amplitude to those observed in vitro upon transfer to the light of dark-adapted, broken chloroplasts incubated in the presence of ATP. We then compared the phosphorylation pattern of thylakoid polypeptides in C. reinhardtii in vitro and in vivo using gamma-[32P]ATP and [32P]orthophosphate labeling, respectively. The same set of polypeptides, mainly light-harvesting complex polypeptides, was phosphorylated in both cases. We observed that this phosphorylation process is reversible and is mediated by the redox state of the plastoquinone pool in vivo as well as in vitro. Similar changes of even larger amplitude were observed with the F34 mutant intact cells lacking in photosystem II centers. The presence of the photosystem II centers is then not required for the occurrence of the plastoquinone-mediated phosphorylation of light-harvesting complex polypeptides.

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