7 results on '"Domonkos, Ildikó"'
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2. Carotenoids, versatile components of oxygenic photosynthesis.
- Author
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Domonkos, Ildikó, Kis, Mihály, Gombos, Zoltán, and Ughy, Bettina
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CAROTENOIDS , *PHOTOSYNTHESIS , *PHYTOENE desaturase , *REACTIVE oxygen species , *ALLOPHYCOCYANIN , *ELONGATION factors (Biochemistry) - Abstract
Abstract: Carotenoids (CARs) are a group of pigments that perform several important physiological functions in all kingdoms of living organisms. CARs serve as protective agents, which are essential structural components of photosynthetic complexes and membranes, and they play an important role in the light harvesting mechanism of photosynthesizing plants and cyanobacteria. The protection against reactive oxygen species, realized by quenching of singlet oxygen and the excited states of photosensitizing molecules, as well as by the scavenging of free radicals, is one of the main biological functions of CARs. X-ray crystallographic localization of CARs revealed that they are present at functionally and structurally important sites of both the PSI and PSII reaction centers. Characterization of a CAR-less cyanobacterial mutant revealed that while the absence of CARs prevents the formation of PSII complexes, it does not abolish the assembly and function of PSI. CAR molecules assist in the formation of protein subunits of the photosynthetic complexes by gluing together their protein components. In addition to their aforementioned indispensable functions, CARs have a substantial role in the formation and maintenance of proper cellular architecture, and potentially also in the protection of the translational machinery under stress conditions. [Copyright &y& Elsevier]
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- 2013
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3. Lipid-assisted protein–protein interactions that support photosynthetic and other cellular activities
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Domonkos, Ildikó, Laczkó-Dobos, Hajnalka, and Gombos, Zoltán
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ELECTRON transport , *X-ray crystallography , *CYANOBACTERIA , *LIPIDS - Abstract
Abstract: Glycoglycerolipids are dominant lipids of photosynthetic organisms, i.e. higher plants and cyanobacteria. X-ray crystallographic localization of glycerolipids revealed that they are present at functionally and structurally important sites of both the PS I and PS II reaction centres. Phosphatidylglycerol (PG) is an indispensible member of glycerolipids, including the formation of functionally active oligomers of the reaction centres both PS I and PS II. Lipids assist in the assembly of protein subunits of the photosynthetic machinery by pasting the individual protein components together. PG is needed to glue CP43 to the reaction centre core. PG and digalactosyldiacylglycerol (DGDG) interact in photosynthetic processes: PG alone controls electron transport at the acceptor site of PS II, and together with DGDG is involved in electron transport at the donor site of PS II. PG is crucial for the formation of division rings and is implicated in the fission of cyanobacteria. [Copyright &y& Elsevier]
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- 2008
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4. Carotenoids are essential for the assembly of cyanobacterial photosynthetic complexes.
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Tóth, Tünde N., Chukhutsina, Volha, Domonkos, Ildikó, Knoppová, Jana, Komenda, Josef, Kis, Mihály, Lénárt, Zsófia, Garab, Győző, Kovács, László, Gombos, Zoltán, and van Amerongen, Herbert
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CAROTENOIDS , *PHOTOSYSTEMS , *CYANOBACTERIA , *COMPLEX compounds , *XANTHOPHYLLS , *OLIGOMERIZATION - Abstract
In photosynthetic organisms, carotenoids (carotenes and xanthophylls) are important for light harvesting, photoprotection and structural stability of a variety of pigment–protein complexes. Here, we investigated the consequences of altered carotenoid composition for the functional organization of photosynthetic complexes in wild-type and various mutant strains of the cyanobacterium Synechocystis sp. PCC 6803. Although it is generally accepted that xanthophylls do not play a role in cyanobacterial photosynthesis in low-light conditions, we have found that the absence of xanthophylls leads to reduced oligomerization of photosystems I and II. This is remarkable because these complexes do not bind xanthophylls. Oligomerization is even more disturbed in crtH mutant cells, which show limited carotenoid synthesis; in these cells also the phycobilisomes are distorted despite the fact that these extramembranous light-harvesting complexes do not contain carotenoids. The number of phycocyanin rods connected to the phycobilisome core is strongly reduced leading to high amounts of unattached phycocyanin units. In the absence of carotenoids the overall organization of the thylakoid membranes is disturbed: Photosystem II is not formed, photosystem I hardly oligomerizes and the assembly of phycobilisomes remains incomplete. These data underline the importance of carotenoids in the structural and functional organization of the cyanobacterial photosynthetic machinery. [ABSTRACT FROM AUTHOR]
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- 2015
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5. Phosphatidylglycerol is implicated in divisome formation and metabolic processes of cyanobacteria.
- Author
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Kóbori, Tímea O., Uzumaki, Tatsuya, Kis, Mihály, Kovács, László, Domonkos, Ildikó, Itoh, Shigeru, Krynická, Vendula, Kuppusamy, Saravanan G., Zakar, Tomas, Dean, Jason, Szilák, László, Komenda, Josef, Gombos, Zoltán, and Ughy, Bettina
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CYANOBACTERIA , *PHOSPHATIDYLGLYCEROL , *PHOTOSYNTHESIS , *CELL division , *BACTERIAL metabolism , *BACTERIA - Abstract
Phosphatidylglycerol is an essential phospholipid for photosynthesis and other cellular processes. We investigated the role of phosphatidylglycerol in cell division and metabolism in a phophatidylglycerol-auxotrophic strain of Synechococcus PCC7942. Here we show that phosphatidylglycerol is essential for the photosynthetic electron transfer and for the oligomerisation of the photosynthetic complexes, notably, we revealed that this lipid is important for non-linear electron transport. Furthermore, we demonstrate that phosphatidylglycerol starvation elevated the expressions of proteins of nitrogen and carbon metabolism. Moreover, we show that phosphatidylglycerol-deficient cells changed the morphology, became elongated, the FtsZ ring did not assemble correctly, and subsequently the division was hindered. However, supplementation with phosphatidylglycerol restored the ring-like structure at the mid-cell region and the normal cell size, demonstrating the phosphatidylglycerol is needed for normal septum formation. Taken together, central roles of phosphatidylglycerol were revealed; it is implicated in the photosynthetic activity, the metabolism and the fission of bacteria. [ABSTRACT FROM AUTHOR]
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- 2018
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6. Two functional sites of phosphatidylglycerol for regulation of reaction of plastoquinone QB in photosystem II
- Author
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Itoh, Shigeru, Kozuki, Takashi, Nishida, Koji, Fukushima, Yoshimasa, Yamakawa, Hisanori, Domonkos, Ildikó, Laczkó-Dobos, Hajnalka, Kis, Mihály, Ughy, Bettina, and Gombos, Zoltán
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PHOSPHATIDYLGLYCEROL , *QUINONE , *ELECTRON transport , *BENZOQUINONES , *CYANOBACTERIA , *SYNECHOCYSTIS - Abstract
Abstract: Functional roles of an anionic lipid phosphatidylglycerol (PG) were studied in pgsA-gene-inactivated and cdsA-gene-inactivated/phycobilisome-less mutant cells of a cyanobacterium Synechocystis sp. PCC 6803, which can grow only in PG-supplemented media. 1) A few days of PG depletion suppressed oxygen evolution of mutant cells supported by p-benzoquinone (BQ). The suppression was recovered slowly in a week after PG re-addition. Measurements of fluorescence yield indicated the enhanced sensitivity of QB to the inactivation by BQ. It is assumed that the loss of low-affinity PG (PGL) enhances the affinity for BQ that inactivates QB. 2) Oxygen evolution without BQ, supported by the endogenous electron acceptors, was slowly suppressed due to the direct inactivation of QB during 10days of PG depletion, and was recovered rapidly within 10h upon the PG re-addition. It is concluded that the loss of high-affinity PG (PGH) displaces QB directly. 3) Electron microscopy images of PG-depleted cells showed the specific suppression of division of mutant cells, which had developed thylakoid membranes attaching phycobilisomes (PBS). 4) Although the PG-depletion for 14days decreased the chlorophyll/PBS ratio to about 1/4, florescence spectra/lifetimes were not modified indicating the flexible energy transfer from PBS to different numbers of PSII. Longer PG-depletion enhanced allophycocyanin fluorescence at 683nm with a long 1.2ns lifetime indicating the suppression of energy transfer from PBS to PSII. 5) Action sites of PGH, PGL and other PG molecules on PSII structure are discussed. [Copyright &y& Elsevier]
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- 2012
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7. Role of phosphatidylglycerol in the function and assembly of Photosystem II reaction center, studied in a cdsA-inactivated PAL mutant strain of Synechocystis sp. PCC6803 that lacks phycobilisomes
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Laczkó-Dobos, Hajnalka, Ughy, Bettina, Tóth, Szilvia Z., Komenda, Josef, Zsiros, Ottó, Domonkos, Ildikó, Párducz, Árpád, Bogos, Balázs, Komura, Masayuki, Itoh, Shigeru, and Gombos, Zoltán
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PHYCOBILISOMES , *CYANOBACTERIA , *THERMOLUMINESCENCE , *METHIONINE - Abstract
Abstract: To analyze the role of phosphatidylglycerol (PG) in photosynthetic membranes of cyanobacteria we used two mutants of Synechocystis sp. PCC6803: the PAL mutant which has no phycobilisomes and shows a high PSII/PSI ratio, and a mutant derived from it by inactivating its cdsA gene encoding cytidine 5''-diphosphate diacylglycerol synthase, a key enzyme in PG synthesis. In a medium supplemented with PG the PAL/ΔcdsA mutant cells grew photoautotrophically. Depletion of PG in the medium resulted (a) in an arrest of cell growth and division, (b) in a slowdown of electron transfer from the acceptor QA to QB in PSII and (c) in a modification of chlorophyll fluorescence curve. The depletion of PG affected neither the redox levels of QA nor the S2 state of the oxygen-evolving manganese complex, as indicated by thermoluminescence studies. Two-dimensional PAGE showed that in the absence of PG (a) the PSII dimer was decomposed into monomers, and (b) the CP43 protein was detached from a major part of the PSII core complex. [35S]-methionine labeling confirmed that PG depletion did not block de novo synthesis of the PSII proteins. We conclude that PG is required for the binding of CP43 within the PSII core complex. [Copyright &y& Elsevier]
- Published
- 2008
- Full Text
- View/download PDF
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