79 research outputs found

    Conservation of core complex subunits shaped the structure and function of photosystem I in the secondary endosymbiont alga Nannochloropsis gaditana

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    Photosystem I (PSI) is a pigment protein complex catalyzing the light-driven electron transport from plastocyanin to ferredoxin in oxygenic photosynthetic organisms. Several PSI subunits are highly conserved in cyanobacteria, algae and plants, whereas others are distributed differentially in the various organisms. Here we characterized the structural and functional properties of PSI purified from the heterokont alga Nannochloropsis gaditana, showing that it is organized as a supercomplex including a core complex and an outer antenna, as in plants and other eukaryotic algae. Differently from all known organisms, the N. gaditana PSI supercomplex contains five peripheral antenna proteins, identified by proteome analysis as type-R light-harvesting complexes (LHCr4-8). Two antenna subunits are bound in a conserved position, as in PSI in plants, whereas three additional antennae are associated with the core on the other side. This peculiar antenna association correlates with the presence of PsaF/J and the absence of PsaH, G and K in the N. gaditana genome and proteome. Excitation energy transfer in the supercomplex is highly efficient, leading to a very high trapping efficiency as observed in all other PSI eukaryotes, showing that although the supramolecular organization of PSI changed during evolution, fundamental functional properties such as trapping efficiency were maintained

    High Light Induced Disassembly of Photosystem II Supercomplexes in Arabidopsis Requires STN7-Dependent Phosphorylation of CP29

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    Photosynthetic oxidation of water and production of oxygen by photosystem II (PSII) in thylakoid membranes of plant chloroplasts is highly affected by changes in light intensities. To minimize damage imposed by excessive sunlight and sustain the photosynthetic activity PSII, organized in supercomplexes with its light harvesting antenna, undergoes conformational changes, disassembly and repair via not clearly understood mechanisms. We characterized the phosphoproteome of the thylakoid membranes from Arabidopsis thaliana wild type, stn7, stn8 and stn7stn8 mutant plants exposed to high light. The high light treatment of the wild type and stn8 caused specific increase in phosphorylation of Lhcb4.1 and Lhcb4.2 isoforms of the PSII linker protein CP29 at five different threonine residues. Phosphorylation of CP29 at four of these residues was not found in stn7 and stn7stn8 plants lacking the STN7 protein kinase. Blue native gel electrophoresis followed by immunological and mass spectrometric analyses of the membrane protein complexes revealed that the high light treatment of the wild type caused redistribution of CP29 from PSII supercomplexes to PSII dimers and monomers. A similar high-light-induced disassembly of the PSII supercomplexes occurred in stn8, but not in stn7 and stn7stn8. Transfer of the high-light-treated wild type plants to normal light relocated CP29 back to PSII supercomplexes. We postulate that disassembly of PSII supercomplexes in plants exposed to high light involves STN7-kinase-dependent phosphorylation of the linker protein CP29. Disruption of this adaptive mechanism can explain dramatically retarded growth of the stn7 and stn7stn8 mutants under fluctuating normal/high light conditions, as previously reported

    Analysis of LhcSR3, a Protein Essential for Feedback De-Excitation in the Green Alga Chlamydomonas reinhardtii

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    To prevent photodamage by excess light, plants use different proteins to sense pH changes and to dissipate excited energy states. In green microalgae, however, the LhcSR3 gene product is able to perform both pH sensing and energy quenching functions

    Reliability and reproducibility of three-dimensional cephalometric landmarks using CBCT: a systematic review

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    Objective : The aim of this study was to review the reliability and reproducibility of 3D-CBCT (cone beam computed tomography) cephalometric landmark identification. Methods : Electronic databases (Pubmed, Scopus, Web of Science) were searched for papers published from 1998 to October 2014. Specific strategies were developed for each database, with the guidance of a librarian. Two reviewers independently analyzed the titles and abstracts for inclusion. The articles that met the inclusion and exclusion criteria were selected for full-text reading, and the selected articles went through methodological quality evaluation. After the exclusion of repeated articles, the titles of the remaining ones were read and 1,328 of them were excluded. The abstracts of 173 articles were read, of which 43 were selected, read in full and submitted to the inclusion and exclusion criteria. Fourteen articles or studies with reliable methodology and reproducibility remained. The data were collected, organized into figures and analyzed for determination of the reliability and reproducibility of the three-dimensional cephalometric landmarks. Results : Overall, the landmarks on the median sagittal line and dental landmarks had the highest reliability, while the landmarks on the condyle, porion and the orbitale presented lower levels of reliability. Point S must be marked in the multiplanar views associated with visualization in 3D reconstruction. Further studies are necessary for evaluating soft tissue landmarks

    Fine control of chlorophyll-carotenoid interactions defines the functionality of light-harvesting proteins in plants

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    V.B. and C.D.P.D. acknowledge the support from the Leverhulme Trust RPG-2015-337. This research utilized Queen Mary’s MidPlus computational facilities, supported by QMUL Research-IT and funded by EPSRC grant EP/K000128/1. W.P.B acknowledges support from the Photosynthetic Antenna Research Center (PARC), an Energy Frontier Research Center funded by the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences under Award DE-SC0001035 for initial development of the TDC calculation code, as well as support from Army Research Office (ARO-MURI) Award W911NF1210420 for further development
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