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Berlin Brandenburg

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  • 1
    Language: English
    In: Plant physiology, April 2015, Vol.167(4), pp.1566-78
    Description: In Chlamydomonas reinhardtii, the LIGHT-HARVESTING COMPLEX STRESS-RELATED PROTEIN3 (LHCSR3) protein is crucial for efficient energy-dependent thermal dissipation of excess absorbed light energy and functionally associates with photosystem II-light-harvesting complex II (PSII-LHCII) supercomplexes. Currently, it is unknown how LHCSR3 binds to the PSII-LHCII supercomplex. In this study, we investigated the role of PHOTOSYSTEM II SUBUNIT R (PSBR) an intrinsic membrane-spanning PSII subunit, in the binding of LHCSR3 to PSII-LHCII supercomplexes. Down-regulation of PSBR expression diminished the efficiency of oxygen evolution and the extent of nonphotochemical quenching and had an impact on the stability of the oxygen-evolving complex as well as on PSII-LHCII-LHCSR3 supercomplex formation. Its down-regulation destabilized the PSII-LHCII supercomplex and strongly reduced the binding of LHCSR3 to PSII-LHCII supercomplexes, as revealed by quantitative proteomics. PHOTOSYSTEM II SUBUNIT P deletion, on the contrary, destabilized PHOTOSYSTEM II SUBUNIT Q binding but did not affect PSBR and LHCSR3 association with PSII-LHCII. In summary, these data provide clear evidence that PSBR is required for the stable binding of LHCSR3 to PSII-LHCII supercomplexes and is essential for efficient energy-dependent quenching and the integrity of the PSII-LHCII-LHCSR3 supercomplex under continuous high light.
    Keywords: Proteomics ; Chlamydomonas Reinhardtii -- Genetics ; Light-Harvesting Protein Complexes -- Metabolism ; Oxygen -- Metabolism ; Photosystem II Protein Complex -- Metabolism
    ISSN: 00320889
    E-ISSN: 1532-2548
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  • 2
    Language: English
    In: Plant physiology, June 2015, Vol.168(2), pp.615-34
    Description: In plants and algae, the serine/threonine kinase STN7/STT7, orthologous protein kinases in Chlamydomonas reinhardtii and Arabidopsis (Arabidopsis thaliana), respectively, is an important regulator in acclimation to changing light environments. In this work, we assessed STT7-dependent protein phosphorylation under high light in C. reinhardtii, known to fully induce the expression of light-harvesting complex stress-related protein3 (LHCSR3) and a nonphotochemical quenching mechanism, in relationship to anoxia where the activity of cyclic electron flow is stimulated. Our quantitative proteomics data revealed numerous unique STT7 protein substrates and STT7-dependent protein phosphorylation variations that were reliant on the environmental condition. These results indicate that STT7-dependent phosphorylation is modulated by the environment and point to an intricate chloroplast phosphorylation network responding in a highly sensitive and dynamic manner to environmental cues and alterations in kinase function. Functionally, the absence of the STT7 kinase triggered changes in protein expression and photoinhibition of photosystem I (PSI) and resulted in the remodeling of photosynthetic complexes. This remodeling initiated a pronounced association of LHCSR3 with PSI-light harvesting complex I (LHCI)-ferredoxin-NADPH oxidoreductase supercomplexes. Lack of STT7 kinase strongly diminished PSII-LHCII supercomplexes, while PSII core complex phosphorylation and accumulation were significantly enhanced. In conclusion, our study provides strong evidence that the regulation of protein phosphorylation is critical for driving successful acclimation to high light and anoxic growth environments and gives new insights into acclimation strategies to these environmental conditions.
    Keywords: Environment ; Photosynthesis ; Chlamydomonas Reinhardtii -- Metabolism ; Multiprotein Complexes -- Metabolism ; Plant Proteins -- Metabolism
    ISSN: 00320889
    E-ISSN: 1532-2548
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  • 3
    Language: English
    In: Plant physiology, October 2018, Vol.178(2), pp.583-595
    Description: In plants, the photosystem I (PSI) core complex stably associates with its light-harvesting chlorophyll / complex I (LHCI) to form the PSI-LHCI supercomplex. The vascular plant PSI core complex associates with four distinct LHCI subunits, whereas that of the green alga binds nine distinct LHCI subunits (LHCA1-LHCA9). The stoichiometry and configuration of these LHCI subunits in the PSI-LHCI supercomplex of remain controversial. Here, we determined the stoichiometry of the nine distinct LHCI subunits relative to PSI subunits through uniform labeling of total proteins using C. We separated the nine LHCI polypeptides by three different sodium dodecyl sulfate-polyacrylamide gel electrophoresis systems. Our data revealed that the PSI-LHCI supercomplex contains two LHCA1 proteins and one of each of the other eight LHCI subunits. Subsequently, we identified their cross-linked products by immunodetection and mass spectrometry to determine the configuration of the 10 LHCI subunits within the PSI-LHCI supercomplex. Furthermore, analyses of PSI-LHCI complexes isolated from Δ and Δ mutants and oligomeric LHCI from a PSI-deficient (Δ/) mutant provided supporting evidence for the LHCI subunit configuration. In conclusion, eight LHCI subunits bind to the PSI core at the site of PSAF subunit in two layers: LHCA1-LHCA8-LHCA7-LHCA3 from PSAG to PSAK, in the inner layer, and LHCA1-LHCA4-LHCA6-LHCA5 in the outer layer. The other two LHCI subunits, LHCA2 and LHCA9, bind PSAB between PSAG and PSAH, PSAG-LHCA9-LHCA2-PSAH. Our study provides new insights into the LHCI configuration linked to the PSI core.
    Keywords: Models, Structural ; Chlamydomonas Reinhardtii -- Metabolism ; Light-Harvesting Protein Complexes -- Metabolism ; Photosystem I Protein Complex -- Metabolism
    E-ISSN: 1532-2548
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  • 4
    Language: English
    Keywords: Demand and Price Analysis ; Food and Agricultural Policy Analysis ; International Trade
    Source: AgEcon Search: Research in Agricultural and Applied Economics
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  • 5
    In: Plant Journal, September 2019, Vol.99(5), pp.877-894
    Description: Phosphorylation dynamics of 3 were investigated in by quantitative proteomics and genetic engineering. 3 protein expression and phosphorylation were induced in high light. Our data revealed synergistic and dynamic N‐terminal 3 phosphorylation. Phosphorylated and nonphosphorylated 3 associated with ‐ supercomplexes. The phosphorylation status of 4 was closely linked to the phosphorylation of multiple sites at the N‐terminus of 3, indicating that 3 phosphorylation may operate as a molecular switch modulating 4 phosphorylation, which in turn is important for ‐ disassembly. Notably, 3 phosphorylation diminished under prolonged high light, which coincided with onset of . Hierarchical clustering of significantly altered proteins revealed similar expression profiles of 3, , and . This finding indicated the existence of a functional link between 3 protein abundance and phosphorylation, photosynthetic electron flow, and the oxidative stress response. We analyzed light‐dependent phosphorylation of LHCSR3 and LHCB4 by quantitative proteomics, genetic engineering, and functional measurements. N‐terminal LHCSR3 phosphorylation is light dependent and modulates phosphorylation of LHCB4 and the association of LHCSR3 with photosynthetic multi‐protein complexes. Our data revealed the functional importance of LHCSR3 phosphorylation, pointing to unforeseen functions in algal photosynthesis.
    Keywords: Photosynthesis ; Light Harvesting ; High Light Stress ; Protein Phosphorylation
    ISSN: 0960-7412
    E-ISSN: 1365-313X
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  • 6
    Language: English
    In: Plant Signaling & Behavior, 02 December 2015, Vol.10(12)
    Description: Light is essential for photosynthesis but excess light is hazardous as it may lead to the formation of reactive oxygen species. Photosynthetic organisms struggle to optimize light utilization and photosynthesis while minimizing photo-oxidative damage. Hereby light to heat dissipation via specialized proteins is a potent mechanism to acclimate toward excess light. In the green alga Chlamydomonas reinhardtii the expression of an ancient light-harvesting protein LHCSR3 enables cells to dissipate harmful excess energy. Herein we summarize newest insights into the function of LHCSR3 from C. reinhardtii.
    Keywords: Chlamydomonas Reinhardtii ; Excess Light to Heat Dissipation ; Light-Harvesting ; Lhcsr3 ; Photosynthesis ; Botany
    E-ISSN: 1559-2324
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  • 7
    Language: English
    In: Frontiers in Plant Science, May 15, 2018
    Description: A number of cell fate determinations, including cell division, cell differentiation, and programmed cell death, intensely occur during plant germline development. How these cell fate determinations are regulated remains largely unclear. The transcription factor E2F is a core cell cycle regulator. Here we show that the Arabidopsis canonical E2Fs, including E2Fa, E2Fb, and E2Fc, play a redundant role in plant germline development. The e2fa e2fb e2fc ( e2fabc ) triple mutant is sterile, although its vegetative development appears normal. On the one hand, the e2fabc microspores undergo cell death during pollen mitosis. Microspores start to die at the bicellular stage. By the tricellular stage, the majority of the e2fabc microspores are degenerated. On the other hand, a wild type ovule often has one megaspore mother cell (MMC), whereas the majority of e2fabc ovules have two to three MMCs. The subsequent female gametogenesis of e2fabc mutant is aborted and the vacuole is severely impaired in the embryo sac. Analysis of transmission efficiency showed that the canonical E2Fs from both male and female gametophyte are essential for plant gametogenesis. Our study reveals that the canonical E2Fs are required for plant germline development, especially the pollen mitosis and the archesporial cell (AC)-MMC transition.
    Keywords: Arabidopsis Thaliana – Physiological Aspects ; Plant Development – Observations
    ISSN: 1664-462X
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  • 8
    Language: English
    In: Archives of Microbiology, 2013, Vol.195(9), pp.637-646
    Description: The effect of Ni 2+ on the growth and functional gene expression of the pure culture and co-culture of Acidithiobacillus thiooxidans and Leptospirillum ferriphilum has been studied. Compared with the pure culture, the co-culture showed a stronger sulfur and ferrous ion oxidation activity. At 100 mM, A. thiooxidans in co-culture grew faster and had 48 h shorter lag phases. The cell number of A. thiooxidans in co-culture was about 5 times higher than that in pure culture. The existence of A. thiooxidans in co-culture activated the expression of some metal resistance genes in L. ferriphilum at least 16 h in advance. A . thiooxidans in co-culture tends to chose more efficient pathways to transport nickel ion, ensuring the export of heavy metal was faster and more effective than that in pure culture. All the data indicated that there were synergetic interactions between iron- and sulfur-oxidizing bacteria under the stress of Ni 2+ .
    Keywords: Acidithiobacillus thiooxidans ; Leptospirillum ferriphilum ; Nickel ; Sulfur oxidation ; Ferrous ion oxidation ; RT-PCR ; Functional gene analysis
    ISSN: 0302-8933
    E-ISSN: 1432-072X
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  • 9
    In: BioMed Research International, 2015, Vol.2015, 13 pages
    Description: The response of iron-oxidizing YSK and sulfur-oxidizing A01 to arsenite under pure culture and coculture was investigated based on biochemical characterization (concentration of iron ion and pH value) and related gene expression. YSK and A01 in pure culture could adapt up to 400 mM and 800 mM As(III) after domestication, respectively, although arsenite showed a negative effect on both strains. The coculture showed a stronger sulfur and ferrous ion oxidation activity when exposed to arsenite. In coculture, the pH value showed no significant difference when under 500 mM arsenite stress, and the cell number of was higher than that in pure culture benefiting from the interaction with . The expression profile showed that the arsenic efflux system in the coculture was more active than that in pure culture, indicating that there is a synergetic interaction between A01 and YSK. In addition, a model was proposed to illustrate the interaction between arsenite and the operon in YSK and A01. This study will facilitate the effective application of coculture in the bioleaching process by taking advantage of strain-strain communication and coordination.
    Keywords: Research Article
    ISSN: 2314-6133
    E-ISSN: 2314-6141
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