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            "title": "Protein kinases and phosphatases involved in the acclimation of the photosynthetic apparatus to a changing light environment",
            "creators": [
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                    "creatorType": "author",
                    "firstName": "Jean-David",
                    "lastName": "Rochaix"
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                {
                    "creatorType": "author",
                    "firstName": "Sylvain",
                    "lastName": "Lemeille"
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                    "creatorType": "author",
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                    "creatorType": "author",
                    "firstName": "Iga",
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            "abstractNote": "Photosynthetic organisms are subjected to frequent changes in light quality and quantity and need to respond accordingly. These acclimatory processes are mediated to a large extent through thylakoid protein phosphorylation. Recently, two major thylakoid protein kinases have been identified and characterized. The Stt7/STN7 kinase is mainly involved in the phosphorylation of the LHCII antenna proteins and is required for state transitions. It is firmly associated with the cytochrome b(6)f complex, and its activity is regulated by the redox state of the plastoquinone pool. The other kinase, Stl1/STN8, is responsible for the phosphorylation of the PSII core proteins. Using a reverse genetics approach, we have recently identified the chloroplast PPH1/TAP38 and PBPC protein phosphatases, which counteract the activity of STN7 and STN8 kinases, respectively. They belong to the PP2C-type phosphatase family and are conserved in land plants and algae. The picture that emerges from these studies is that of a complex regulatory network of chloroplast protein kinases and phosphatases that is involved in light acclimation, in maintenance of the plastoquinone redox poise under fluctuating light and in the adjustment to metabolic needs.",
            "publicationTitle": "Philosophical transactions of the Royal Society of London. Series B, Biological sciences",
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            "date": "Dec 19, 2012",
            "volume": "367",
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                    "tag": "Acclimatization",
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                },
                {
                    "tag": "Amino Acid Sequence",
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                },
                {
                    "tag": "Arabidopsis",
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                    "tag": "Arabidopsis Proteins",
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                {
                    "tag": "Chlamydomonas reinhardtii",
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                    "tag": "Chloroplasts",
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                    "tag": "Environment",
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                    "tag": "Light",
                    "type": 1
                },
                {
                    "tag": "Light-Harvesting Protein Complexes",
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                {
                    "tag": "Molecular Sequence Data",
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                {
                    "tag": "Oxidation-Reduction",
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                    "tag": "Phosphoprotein Phosphatases",
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                    "tag": "Phosphorylation",
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                {
                    "tag": "Photosynthesis",
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                },
                {
                    "tag": "Photosystem II Protein Complex",
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                },
                {
                    "tag": "Plastoquinone",
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                },
                {
                    "tag": "Protein Kinases",
                    "type": 1
                },
                {
                    "tag": "Protein-Serine-Threonine Kinases",
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                }
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            "creatorSummary": "Horton",
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            "version": 2,
            "itemType": "journalArticle",
            "title": "Optimization of light harvesting and photoprotection: molecular mechanisms and physiological consequences",
            "creators": [
                {
                    "creatorType": "author",
                    "firstName": "Peter",
                    "lastName": "Horton"
                }
            ],
            "abstractNote": "The distinctive lateral organization of the protein complexes in the thylakoid membrane investigated by Jan Anderson and co-workers is dependent on the balance of various attractive and repulsive forces. Modulation of these forces allows critical physiological regulation of photosynthesis that provides efficient light-harvesting in limiting light but dissipation of excess potentially damaging radiation in saturating light. The light-harvesting complexes (LHCII) are central to this regulation, which is achieved by phosphorylation of stromal residues, protonation on the lumen surface and de-epoxidation of bound violaxanthin. The functional flexibility of LHCII derives from a remarkable pigment composition and configuration that not only allow efficient absorption of light and efficient energy transfer either to photosystem II or photosystem I core complexes, but through subtle configurational changes can also exhibit highly efficient dissipative reactions involving chlorophyll-xanthophyll and/or chlorophyll-chlorophyll interactions. These changes in function are determined at a macroscopic level by alterations in protein-protein interactions in the thylakoid membrane. The capacity and dynamics of this regulation are tuned to different physiological scenarios by the exact protein and pigment content of the light-harvesting system. Here, the molecular mechanisms involved will be reviewed, and the optimization of the light-harvesting system in different environmental conditions described.",
            "publicationTitle": "Philosophical transactions of the Royal Society of London. Series B, Biological sciences",
            "publisher": "",
            "place": "",
            "date": "Dec 19, 2012",
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            "pages": "3455-3465",
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            "DOI": "10.1098/rstb.2012.0069",
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                },
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                    "tag": "Cold Temperature",
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                    "tag": "Photosystem I Protein Complex",
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                {
                    "tag": "Photosystem II Protein Complex",
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                {
                    "tag": "Protein Interaction Mapping",
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                    "tag": "Sunlight",
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                {
                    "tag": "Thylakoids",
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                {
                    "tag": "Xanthophylls",
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            ],
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            "dateAdded": "2013-10-22T09:53:01Z",
            "dateModified": "2013-10-22T09:53:01Z"
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