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Thomas S Bibby - One of the best experts on this subject based on the ideXlab platform.
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supramolecular organization of phycobiliproteins in the chlorophyll d containing cyanobacterium acaryochloris marina
FEBS Letters, 2009Co-Authors: Min Chen, Matthias Floetenmeyer, Thomas S BibbyAbstract:Here we report the high-resolution detail of the organization of phycobiliprotein structures associated with photosynthetic membranes of the chlorophyll d-containing cyanobacterium Acaryochloris marina. Cryo-electron transmission-microscopy on native cell sections show extensive patches of near-crystalline phycobiliprotein rods that are associated with the stromal side of photosynthetic membranes. This supramolecular photosynthetic structure represents a novel mechanism of organizing the photosynthetic light-harvesting machinery. In addition, the specific location of phycobiliprotein patches suggests a physical separation of photosystem I and photosystem II reaction centres. Based on this finding and the known photosystem's structure in Acaryochloris, we discuss possible membrane arrangements of photosynthetic membrane complexes in this species.
Tomas Morosinotto - One of the best experts on this subject based on the ideXlab platform.
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Higher order photoprotection mutants reveal the importance of ΔpH-dependent photosynthesis-control in preventing light induced damage to both photosystem II and photosystem I
'Springer Science and Business Media LLC', 2020Co-Authors: R. Barbato, Tomas Morosinotto, L. Tadini, R. Cannata, C. Peracchio, N. Jeran, A. Alboresi, A.a. Bajwa, V. Paakkarinen, M. SuorsaAbstract:Although light is essential for photosynthesis, when in excess, it may damage the photosynthetic apparatus, leading to a phenomenon known as photoinhibition. Photoinhibition was thought as a light-induced damage to photosystem II; however, it is now clear that even photosystem I may become very vulnerable to light. One main characteristic of light induced damage to photosystem II (PSII) is the increased turnover of the reaction center protein, D1: when rate of degradation exceeds the rate of synthesis, loss of PSII activity is observed. With respect to photosystem I (PSI), an excess of electrons, instead of an excess of light, may be very dangerous. Plants possess a number of mechanisms able to prevent, or limit, such damages by safe thermal dissipation of light energy (non-photochemical quenching, NPQ), slowing-down of electron transfer through the intersystem transport chain (photosynthesis-control, PSC) in co-operation with the Proton Gradient Regulation (PGR) proteins, PGR5 and PGRL1, collectively called as short-term photoprotection mechanisms, and the redistribution of light between Photosystems, called state transitions (responsible of fluorescence quenching at PSII, qT), is superimposed to these short term photoprotective mechanisms. In this manuscript we have generated a number of higher order mutants by crossing genotypes carrying defects in each of the short-term photoprotection mechanisms, with the final aim to obtain a direct comparison of their role and efficiency in photoprotection. We found that mutants carrying a defect in the \u394pH-dependent photosynthesis-control are characterized by photoinhibition of both Photosystems, irrespectively of whether PSBS-dependent NPQ or state transitions defects were present or not in the same individual, demonstrating the primary role of PSC in photoprotection. Moreover, mutants with a limited capability to develop a strong PSBS-dependent NPQ, were characterized by a high turnover of the D1 protein and high values of Y(NO), which might reflect energy quenching processes occurring within the PSII reaction center
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Characterization of the photosynthetic apparatus of the Eustigmatophycean Nannochloropsis gaditana: evidence of convergent evolution in the supramolecular organization of photosystem I.
Biochimica et biophysica acta, 2013Co-Authors: Stefania Basso, Diana Simionato, Caterina Gerotto, Anna Segalla, Giorgio M. Giacometti, Tomas MorosinottoAbstract:Nannochloropsis gaditana belongs to Eustigmatophyceae, a class of eukaryotic algae resulting from a secondary endosymbiotic event. Species of this class have been poorly characterized thus far but are now raising increasing interest in the scientific community because of their possible application in biofuel production. Nannochloropsis species have a peculiar photosynthetic apparatus characterized by the presence of only chlorophyll a, with violaxanthin and vaucheriaxanthin esters as the most abundant carotenoids. In this study, the photosynthetic apparatus of this species was analyzed by purifying the thylakoids and isolating the different pigment-binding complexes upon mild solubilization. The results from the biochemical and spectroscopic characterization showed that the photosystem II antenna is loosely bound to the reaction center, whereas the association is stronger in photosystem I, with the antenna-reaction center super-complexes surviving purification. Such a supramolecular organization was found to be conserved in photosystem I from several other photosynthetic eukaryotes, even though these taxa are evolutionarily distant. A hypothesis on the possible selective advantage of different associations of the antenna complexes of Photosystems I and II is discussed.
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a red shifted antenna protein associated with photosystem ii in physcomitrella patens
Journal of Biological Chemistry, 2011Co-Authors: A. Alboresi, Caterina Gerotto, Stefano Cazzaniga, Roberto Bassi, Tomas MorosinottoAbstract:Antenna systems of plants and green algae are made up of pigment-protein complexes belonging to the light-harvesting complex (LHC) multigene family. LHCs increase the light-harvesting cross-section of Photosystems I and II and catalyze photoprotective reactions that prevent light-induced damage in an oxygenic environment. The genome of the moss Physcomitrella patens contains two genes encoding LHCb9, a new antenna protein that bears an overall sequence similarity to photosystem II antenna proteins but carries a specific motif typical of photosystem I antenna proteins. This consists of the presence of an asparagine residue as a ligand for Chl 603 (A5) chromophore rather than a histidine, the common ligand in all other LHCbs. Asparagine as a Chl 603 (A5) ligand generates red-shifted spectral forms associated with photosystem I rather than with photosystem II, suggesting that in P. patens, the energy landscape of photosystem II might be different with respect to that of most green algae and plants. In this work, we show that the in vitro refolded LHCb9-pigment complexes carry a red-shifted fluorescence emission peak, different from all other known photosystem II antenna proteins. By using a specific antibody, we localized LHCb9 within PSII supercomplexes in the thylakoid membranes. This is the first report of red-shifted spectral forms in a PSII antenna system, suggesting that this biophysical feature might have a special role either in optimization of light use efficiency or in photoprotection in the specific environmental conditions experienced by this moss.
Roberto Bassi - One of the best experts on this subject based on the ideXlab platform.
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light harvesting complex stress related proteins catalyze excess energy dissipation in both Photosystems of physcomitrella patens
The Plant Cell, 2015Co-Authors: Alberta Pinnola, Stefano Cazzaniga, A. Alboresi, Reinat Nevo, Smadar Levinzaidman, Ziv Reich, Roberto BassiAbstract:Two LHC-like proteins, Photosystem II Subunit S (PSBS) and Light-Harvesting Complex Stress-Related (LHCSR), are essential for triggering excess energy dissipation in chloroplasts of vascular plants and green algae, respectively. The mechanism of quenching was studied in Physcomitrella patens, an early divergent streptophyta (including green algae and land plants) in which both proteins are active. PSBS was localized in grana together with photosystem II (PSII), but LHCSR was located mainly in stroma-exposed membranes together with photosystem I (PSI), and its distribution did not change upon high-light treatment. The quenched conformation can be preserved by rapidly freezing the high-light-treated tissues in liquid nitrogen. When using green fluorescent protein as an internal standard, 77K fluorescence emission spectra on isolated chloroplasts allowed for independent assessment of PSI and PSII fluorescence yield. Results showed that both Photosystems underwent quenching upon high-light treatment in the wild type in contrast to mutants depleted of LHCSR, which lacked PSI quenching. Due to the contribution of LHCII, P. patens had a PSI antenna size twice as large with respect to higher plants. Thus, LHCII, which is highly abundant in stroma membranes, appears to be the target of quenching by LHCSR.
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a red shifted antenna protein associated with photosystem ii in physcomitrella patens
Journal of Biological Chemistry, 2011Co-Authors: A. Alboresi, Caterina Gerotto, Stefano Cazzaniga, Roberto Bassi, Tomas MorosinottoAbstract:Antenna systems of plants and green algae are made up of pigment-protein complexes belonging to the light-harvesting complex (LHC) multigene family. LHCs increase the light-harvesting cross-section of Photosystems I and II and catalyze photoprotective reactions that prevent light-induced damage in an oxygenic environment. The genome of the moss Physcomitrella patens contains two genes encoding LHCb9, a new antenna protein that bears an overall sequence similarity to photosystem II antenna proteins but carries a specific motif typical of photosystem I antenna proteins. This consists of the presence of an asparagine residue as a ligand for Chl 603 (A5) chromophore rather than a histidine, the common ligand in all other LHCbs. Asparagine as a Chl 603 (A5) ligand generates red-shifted spectral forms associated with photosystem I rather than with photosystem II, suggesting that in P. patens, the energy landscape of photosystem II might be different with respect to that of most green algae and plants. In this work, we show that the in vitro refolded LHCb9-pigment complexes carry a red-shifted fluorescence emission peak, different from all other known photosystem II antenna proteins. By using a specific antibody, we localized LHCb9 within PSII supercomplexes in the thylakoid membranes. This is the first report of red-shifted spectral forms in a PSII antenna system, suggesting that this biophysical feature might have a special role either in optimization of light use efficiency or in photoprotection in the specific environmental conditions experienced by this moss.
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analysis of the chloroplast protein kinase stt7 during state transitions
PLOS Biology, 2009Co-Authors: Sylvain Lemeille, Nathalie Depegefargeix, Christian Delessert, Adrian Willig, Roberto Bassi, Jean David RochaixAbstract:State transitions allow for the balancing of the light excitation energy between photosystem I and photosystem II and for optimal photosynthetic activity when photosynthetic organisms are subjected to changing light conditions. This process is regulated by the redox state of the plastoquinone pool through the Stt7/STN7 protein kinase required for phosphorylation of the light-harvesting complex LHCII and for the reversible displacement of the mobile LHCII between the Photosystems. We show that Stt7 is associated with photosynthetic complexes including LHCII, photosystem I, and the cytochrome b6f complex. Our data reveal that Stt7 acts in catalytic amounts. We also provide evidence that Stt7 contains a transmembrane region that separates its catalytic kinase domain on the stromal side from its N-terminal end in the thylakoid lumen with two conserved Cys that are critical for its activity and state transitions. On the basis of these data, we propose that the activity of Stt7 is regulated through its transmembrane domain and that a disulfide bond between the two lumen Cys is essential for its activity. The high-light–induced reduction of this bond may occur through a transthylakoid thiol–reducing pathway driven by the ferredoxin-thioredoxin system which is also required for cytochrome b6f assembly and heme biogenesis.
Stefano Cazzaniga - One of the best experts on this subject based on the ideXlab platform.
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photosystem ii antenna complexes cp26 and cp29 are essential for nonphotochemical quenching in chlamydomonas reinhardtii
Plant Cell and Environment, 2020Co-Authors: Stefano Cazzaniga, Jooyoen Jeong, Andrea Pompa, Francesco Bellamoli, Federico Perozeni, Matteo BallottariAbstract:: Photosystems must balance between light harvesting to fuel the photosynthetic process for CO2 fixation and mitigating the risk of photodamage due to absorption of light energy in excess. Eukaryotic photosynthetic organisms evolved an array of pigment-binding proteins called light harvesting complexes constituting the external antenna system in the Photosystems, where both light harvesting and activation of photoprotective mechanisms occur. In this work, the balancing role of CP29 and CP26 photosystem II antenna subunits was investigated in Chlamydomonas reinhardtii using CRISPR-Cas9 technology to obtain single and double mutants depleted of monomeric antennas. Absence of CP26 and CP29 impaired both photosynthetic efficiency and photoprotection: Excitation energy transfer from external antenna to reaction centre was reduced, and state transitions were completely impaired. Moreover, differently from higher plants, photosystem II monomeric antenna proteins resulted to be essential for photoprotective thermal dissipation of excitation energy by nonphotochemical quenching.
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functional analysis of photosynthetic pigment binding complexes in the green alga haematococcus pluvialis reveals distribution of astaxanthin in Photosystems
Scientific Reports, 2017Co-Authors: Francesco Mascia, Federico Perozeni, Stefano Cazzaniga, Laura Girolomoni, Marcelo J P Alcocer, Ilaria Bargigia, Giulio Cerullo, Cosimo Dandrea, Matteo BallottariAbstract:Astaxanthin is a ketocarotenoid produced by photosynthetic microalgae. It is a pigment of high industrial interest in acquaculture, cosmetics, and nutraceutics due to its strong antioxidant power. Haematococcus pluvialis, a fresh-water microalga, accumulates high levels of astaxanthin upon oxidative stress, reaching values up to 5% per dry weight. H. pluvialis accumulates astaxanthin in oil droplets in the cytoplasm, while the chloroplast volume is reduced. In this work, we investigate the biochemical and spectroscopic properties of the H. pluvialis pigment binding complexes responsible for light harvesting and energy conversion. Our findings demonstrate that the main features of chlorophyll and carotenoid binding complexes previously reported for higher plants or Chlamydomonas reinhardtii are preserved under control conditions. Transition to astaxanthin rich cysts however leads to destabilization of the Photosystems. Surprisingly, astaxanthin was found to be bound to both Photosystem I and II, partially substituting β-carotene, and thus demonstrating possible astaxanthin biosynthesis in the plastids or transport from the cytoplasm to the chloroplast. Astaxanthin binding to Photosystems does not however improve their photoprotection, but rather reduces the efficiency of excitation energy transfer to the reaction centers. We thus propose that astaxanthin binding partially destabilizes Photosystem I and II.
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light harvesting complex stress related proteins catalyze excess energy dissipation in both Photosystems of physcomitrella patens
The Plant Cell, 2015Co-Authors: Alberta Pinnola, Stefano Cazzaniga, A. Alboresi, Reinat Nevo, Smadar Levinzaidman, Ziv Reich, Roberto BassiAbstract:Two LHC-like proteins, Photosystem II Subunit S (PSBS) and Light-Harvesting Complex Stress-Related (LHCSR), are essential for triggering excess energy dissipation in chloroplasts of vascular plants and green algae, respectively. The mechanism of quenching was studied in Physcomitrella patens, an early divergent streptophyta (including green algae and land plants) in which both proteins are active. PSBS was localized in grana together with photosystem II (PSII), but LHCSR was located mainly in stroma-exposed membranes together with photosystem I (PSI), and its distribution did not change upon high-light treatment. The quenched conformation can be preserved by rapidly freezing the high-light-treated tissues in liquid nitrogen. When using green fluorescent protein as an internal standard, 77K fluorescence emission spectra on isolated chloroplasts allowed for independent assessment of PSI and PSII fluorescence yield. Results showed that both Photosystems underwent quenching upon high-light treatment in the wild type in contrast to mutants depleted of LHCSR, which lacked PSI quenching. Due to the contribution of LHCII, P. patens had a PSI antenna size twice as large with respect to higher plants. Thus, LHCII, which is highly abundant in stroma membranes, appears to be the target of quenching by LHCSR.
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a red shifted antenna protein associated with photosystem ii in physcomitrella patens
Journal of Biological Chemistry, 2011Co-Authors: A. Alboresi, Caterina Gerotto, Stefano Cazzaniga, Roberto Bassi, Tomas MorosinottoAbstract:Antenna systems of plants and green algae are made up of pigment-protein complexes belonging to the light-harvesting complex (LHC) multigene family. LHCs increase the light-harvesting cross-section of Photosystems I and II and catalyze photoprotective reactions that prevent light-induced damage in an oxygenic environment. The genome of the moss Physcomitrella patens contains two genes encoding LHCb9, a new antenna protein that bears an overall sequence similarity to photosystem II antenna proteins but carries a specific motif typical of photosystem I antenna proteins. This consists of the presence of an asparagine residue as a ligand for Chl 603 (A5) chromophore rather than a histidine, the common ligand in all other LHCbs. Asparagine as a Chl 603 (A5) ligand generates red-shifted spectral forms associated with photosystem I rather than with photosystem II, suggesting that in P. patens, the energy landscape of photosystem II might be different with respect to that of most green algae and plants. In this work, we show that the in vitro refolded LHCb9-pigment complexes carry a red-shifted fluorescence emission peak, different from all other known photosystem II antenna proteins. By using a specific antibody, we localized LHCb9 within PSII supercomplexes in the thylakoid membranes. This is the first report of red-shifted spectral forms in a PSII antenna system, suggesting that this biophysical feature might have a special role either in optimization of light use efficiency or in photoprotection in the specific environmental conditions experienced by this moss.
Dario Leister - One of the best experts on this subject based on the ideXlab platform.
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photosystem ii core phosphorylation and photosynthetic acclimation require two different protein kinases
Nature, 2005Co-Authors: Thomas Pfannschmidt, Vera Bonardi, Paolo Pesaresi, Thomas Becker, Enrico Schleiff, Raik Wagner, Peter Jahns, Dario LeisterAbstract:Illumination changes elicit modifications of thylakoid proteins and reorganization of the photosynthetic machinery. This involves, in the short term, phosphorylation of photosystem II (PSII) and light-harvesting (LHCII) proteins. PSII phosphorylation is thought to be relevant for PSII turnover, whereas LHCII phosphorylation is associated with the relocation of LHCII and the redistribution of excitation energy (state transitions) between Photosystems. In the long term, imbalances in energy distribution between Photosystems are counteracted by adjusting photosystem stoichiometry. In the green alga Chlamydomonas and the plant Arabidopsis, state transitions require the orthologous protein kinases STT7 and STN7, respectively. Here we show that in Arabidopsis a second protein kinase, STN8, is required for the quantitative phosphorylation of PSII core proteins. However, PSII activity under high-intensity light is affected only slightly in stn8 mutants, and D1 turnover is indistinguishable from the wild type, implying that reversible protein phosphorylation is not essential for PSII repair. Acclimation to changes in light quality is defective in stn7 but not in stn8 mutants, indicating that short-term and long-term photosynthetic adaptations are coupled. Therefore the phosphorylation of LHCII, or of an unknown substrate of STN7, is also crucial for the control of photosynthetic gene expression.
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Knock-Out of the Genes Coding for the Rieske Protein and the ATP-Synthase δ-Subunit of Arabidopsis. Effects on Photosynthesis, Thylakoid Protein Composition, and Nuclear Chloroplast Gene Expression
Plant physiology, 2003Co-Authors: Daniela Maiwald, Paolo Pesaresi, Peter Jahns, Angela Dietzmann, Anne Joliot, Joshua Z. Levin, Francesco Salamini, Dario LeisterAbstract:In Arabidopsis, the nuclear genes PetC and AtpD code for the Rieske protein of the cytochrome b6/f (cyt b6/f) complex and the δ-subunit of the chloroplast ATP synthase (cpATPase), respectively. Knock-out alleles for each of these loci have been identified. Greenhouse-grown petc-2 and atpd-1 mutants are seedling lethal, whereas heterotrophically propagated plants display a high-chlorophyll (Chl)-fluorescence phenotype, indicating that the products of PetC and AtpD are essential for photosynthesis. Additional effects of the mutations in axenic culture include altered leaf coloration and increased photosensitivity. Lack of the Rieske protein affects the stability of cyt b6/f and influences the level of other thylakoid proteins, particularly those of photosystem II. In petc-2, linear electron flow is blocked, leading to an altered redox state of both the primary quinone acceptor QA in photosystem II and the reaction center Chl P700 in photosystem I. Absence of cpATPase-δ destabilizes the entire cpATPase complex, whereas residual accumulation of cyt b6/f and of the Photosystems still allows linear electron flow. In atpd-1, the increase in non-photochemical quenching of Chl fluorescence and a higher de-epoxidation state of xanthophyll cycle pigments under low light is compatible with a slower dissipation of the transthylakoid proton gradient. Further and clear differences between the two mutations are evident when mRNA expression profiles of nucleus-encoded chloroplast proteins are considered, suggesting that the physiological states conditioned by the two mutations trigger different modes of plastid signaling and nuclear response.
