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1 Niyogi, K.K., Truong, T.B., Evolution of flexible non-photochemical quenching mechanisms that regulate light harvesting in oxygenic photosynthesis. Curr. Opin. Plant Biol. 16 (2013), 307–314.
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3 Kirilovsky, D., Kerfeld, C.A., Cyanobacterial photoprotection by the orange carotenoid protein. Nat. Plants, 2, 2016, 16180.
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4 Kirilovsky, D., Kerfeld, C.A., The Orange Carotenoid Protein: a blue-green light photoactive protein. Photochem. Photobiol. Sci. 12 (2013), 1135–1143.
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5 Liu, H., Zhang, H., Niedzwiedzki, D.M., Prado, M., He, G., Gross, M.L., Blankenship, R.E., Phycobilisomes supply excitations to both photosystems in a megacomplex in cyanobacteria. Science 342 (2013), 1104–1107.
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Liu, H.1
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6
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0037226278
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The crystal structure of a cyanobacterial water-soluble carotenoid binding protein
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2, discovered its structural domains could be encoded as separate genes, noted its ability to change color to red, suggested it would be suitable for a photoprotective function.
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2, discovered its structural domains could be encoded as separate genes, noted its ability to change color to red, suggested it would be suitable for a photoprotective function.
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Kerfeld, C.A.1
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7
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The cyanobacterial photoactive orange carotenoid protein is an excellent singlet oxygen quencher
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7 Sedoud, A., Lopez-Igual, R., Rehman, A.U., Wilson, A., Perreau, F., Boulay, C., Vass, I., Krieger-Liszkay, A., Kirilovsky, D., The cyanobacterial photoactive orange carotenoid protein is an excellent singlet oxygen quencher. Plant Cell 26 (2014), 1781–1791.
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Sedoud, A.1
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8
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8 Kerfeld, C.A., Structure and function of the water-soluble carotenoid-binding proteins of cyanobacteria. Photosynth. Res. 81 (2004), 215–225.
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Kerfeld, C.A.1
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9
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This work identified and classified OCP, FRP, HCP, and CTDH genes co-occurring among cyanobacterial genomes, phylogenomically subclassified OCP-NTD homologs into distinct paralogous HCP subclades, revealed divergent expression patterns among HCP subtypes, and introduced a hypothesis for OCP evolution involving ancient domain fusion of a CTDH with an HCP4-like ancestor. The first crystal structures of an HCP are also presented, using HCP1 from Nostoc 7120, demonstrating flexible binding of a range of carotenoids.
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9•• Melnicki, M.R., Leverenz, R.L., Sutter, M., Lopez-Igual, R., Wilson, A., Pawlowski, E.G., Perreau, F., Kirilovsky, D., Kerfeld, C.A., Structure, diversity, and evolution of a new family of soluble carotenoid-binding proteins in cyanobacteria. Mol. Plant 9 (2016), 1379–1394 This work identified and classified OCP, FRP, HCP, and CTDH genes co-occurring among cyanobacterial genomes, phylogenomically subclassified OCP-NTD homologs into distinct paralogous HCP subclades, revealed divergent expression patterns among HCP subtypes, and introduced a hypothesis for OCP evolution involving ancient domain fusion of a CTDH with an HCP4-like ancestor. The first crystal structures of an HCP are also presented, using HCP1 from Nostoc 7120, demonstrating flexible binding of a range of carotenoids.
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Melnicki, M.R.1
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10
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84977581459
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Different functions of the paralogs to the N-terminal domain of the orange carotenoid protein in the cyanobacterium Anabaena sp. PCC 7120
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2 quenchers). Native HCP expression and subcellular localization patterns were examined and supported evidence for subfunctionalization.
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2 quenchers). Native HCP expression and subcellular localization patterns were examined and supported evidence for subfunctionalization.
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Lopez-Igual, R.1
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11
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77953313030
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11 Wilson, A., Kinney, J.N., Zwart, P.H., Punginelli, C., D'Haene, S., Perreau, F., Klein, M.G., Kirilovsky, D., Kerfeld, C.A., Structural determinants underlying photoprotection in the photoactive orange carotenoid protein of cyanobacteria. J. Biol. Chem. 285 (2010), 18364–18375.
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12
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50149083653
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A photoactive carotenoid protein acting as light intensity sensor
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12 Wilson, A., Punginelli, C., Gall, A., Bonetti, C., Alexandre, M., Routaboul, J.M., Kerfeld, C.A., van Grondelle, R., Robert, B., Kennis, J.T., et al. A photoactive carotenoid protein acting as light intensity sensor. Proc. Natl. Acad. Sci. U. S. A. 105 (2008), 12075–12080.
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13
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13 Bourcier de Carbon, C., Thurotte, A., Wilson, A., Perreau, F., Kirilovsky, D., Biosynthesis of soluble carotenoid holoproteins in Escherichia coli. Sci. Rep., 5, 2015, 9085.
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14
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14 Mori, Y., Computational study on the color change of 3′-hydroxyechinenone in the orange carotenoid protein. Chem. Phys. Lett. 652 (2016), 184–189.
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15 Wilson, A., Punginelli, C., Couturier, M., Perreau, F., Kirilovsky, D., Essential role of two tyrosines and two tryptophans on the photoprotection activity of the Orange Carotenoid Protein. Biochim. Biophys. Acta 1807 (2011), 293–301.
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16
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16 Punginelli, C., Wilson, A., Routaboul, J.M., Kirilovsky, D., Influence of zeaxanthin and echinenone binding on the activity of the orange carotenoid protein. Biochim. Biophys. Acta 1787 (2009), 280–288.
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17
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17 Zhang, H., Liu, H., Niedzwiedzki, D.M., Prado, M., Jiang, J., Gross, M.L., Blankenship, R.E., Molecular mechanism of photoactivation and structural location of the cyanobacterial orange carotenoid protein. Biochemistry 53 (2014), 13–19.
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18
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84944080519
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Local and global structural drivers for the photoactivation of the orange carotenoid protein
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R crystals, and identified both global and local structural changes upon photoactivation, including complete domain dissociation, unfolding of the N-terminal extension and its dissociation from the CTD, and rearrangement of the H-bonding network associated with conserved residues and structurally-relevant water molecules.
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R crystals, and identified both global and local structural changes upon photoactivation, including complete domain dissociation, unfolding of the N-terminal extension and its dissociation from the CTD, and rearrangement of the H-bonding network associated with conserved residues and structurally-relevant water molecules.
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Gupta, S.1
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19
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19 Leverenz, R.L., Jallet, D., Li, M.D., Mathies, R.A., Kirilovsky, D., Kerfeld, C.A., Structural and functional modularity of the orange carotenoid protein: distinct roles for the N- and C-terminal domains in cyanobacterial photoprotection. Plant Cell 26 (2014), 426–437.
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20
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PHOTOSYNTHESIS. A 12 Å carotenoid translocation in a photoswitch associated with cyanobacterial photoprotection
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R-like optical and quenching properties, indicating that photoactivation of full-length OCP is accompanied by a 12 Å translocation of the carotenoid molecule further into the NTD.
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R-like optical and quenching properties, indicating that photoactivation of full-length OCP is accompanied by a 12 Å translocation of the carotenoid molecule further into the NTD.
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21 Wu, Y.P., Krogmann, D.W., The orange carotenoid protein of Synechocystis PCC 6803. Biochim. Biophys. Acta 1322 (1997), 1–7.
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22 Fraikin, G.Y., Strakhovskaya, M.G., Belenikina, N.S., Rubin, A.B., Bacterial photosensory proteins: regulatory functions and optogenetic applications. Microbiology 84 (2015), 461–472.
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24
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24 Maksimov, E.G., Shirshin, E.A., Sluchanko, N.N., Zlenko, D.V., Parshina, E.Y., Tsoraev, G.V., Klementiev, K.E., Budylin, G.S., Schmitt, F.J., Friedrich, T., et al. The signaling state of orange carotenoid protein. Biophys. J. 109 (2015), 595–607.
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25
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25 Liu, H., Zhang, H., King, J.D., Wolf, N.R., Prado, M., Gross, M.L., Blankenship, R.E., Mass spectrometry footprinting reveals the structural rearrangements of cyanobacterial orange carotenoid protein upon light activation. Biochim. Biophys. Acta 1837 (2014), 1955–1963.
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26
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26 Thurotte, A., Lopez-Igual, R., Wilson, A., Comolet, L., Bourcier de Carbon, C., Xiao, F., Kirilovsky, D., Regulation of orange carotenoid protein activity in cyanobacterial photoprotection. Plant Physiol. 169 (2015), 737–747.
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27
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27 De Re, E., Schlau-Cohen, G.S., Leverenz, R.L., Huxter, V.M., Oliver, T.A., Mathies, R.A., Fleming, G.R., Insights into the structural changes occurring upon photoconversion in the orange carotenoid protein from broadband two-dimensional electronic spectroscopy. J. Phys. Chem. B 118 (2014), 5382–5389.
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28
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28 Maksimov, E.G., Moldenhauer, M., Shirshin, E.A., Parshina, E.A., Sluchanko, N.N., Klementiev, K.E., Tsoraev, G.V., Tavraz, N.N., Willoweit, M., Schmitt, F.-J., et al. A comparative study of three signaling forms of the orange carotenoid protein. Photosynth. Res. 130 (2016), 389–401.
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29
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29 Zhang, H., Liu, H., Lu, Y., Wolf, N.R., Gross, M.L., Blankenship, R.E., Native mass spectrometry and ion mobility characterize the orange carotenoid protein functional domains. Biochim. Biophys. Acta 1857 (2016), 734–739.
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30
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30 Cogdell, R.J., Gardiner, A.T., Activated OCP unlocks nonphotochemical quenching in cyanobacteria. Proc. Natl. Acad. Sci. U. S. A. 112 (2015), 12547–12548.
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31
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31 Boulay, C., Wilson, A., D'Haene, S., Kirilovsky, D., Identification of a protein required for recovery of full antenna capacity in OCP-related photoprotective mechanism in cyanobacteria. Proc. Natl. Acad. Sci. U. S. A. 107 (2010), 11620–11625.
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32 Gwizdala, M., Wilson, A., Omairi-Nasser, A., Kirilovsky, D., Characterization of the Synechocystis PCC 6803 Fluorescence Recovery Protein involved in photoprotection. Biochim. Biophys. Acta 1827 (2013), 348–354.
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33
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This work determined the first FRP crystal structure, observing two different oligomeric configurations within the same asymmetric unit, each with a different fold topology within the respective monomers. Bioinformatics and structural analysis suggested that the dimer is the active form and functional and biochemical analyses of site-directed mutants identified critical residues as well as a possible active site.
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33•• Sutter M, M., Wilson, A., Leverenz, R.L., Lopez-Igual, R., Thurotte, A., Salmeen, A.E., Kirilovsky, D., Kerfeld, C.A., Crystal structure of the FRP and identification of the active site for modulation of OCP-mediated photoprotection in cyanobacteria. Proc. Natl. Acad. Sci. U. S. A. 110 (2013), 10022–10027 This work determined the first FRP crystal structure, observing two different oligomeric configurations within the same asymmetric unit, each with a different fold topology within the respective monomers. Bioinformatics and structural analysis suggested that the dimer is the active form and functional and biochemical analyses of site-directed mutants identified critical residues as well as a possible active site.
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34
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34 Lu, Y., Liu, H., Saer, R., Zhang, H., Meyer, C., Li, V.L., Shi, L., King, J.D., Gross, M.L., Blankenship, R.E., Native mass spectrometry analysis of oligomerization states of FRP and OCP: two proteins involved in the cyanobacterial photoprotection cycle. Biochemistry 56 (2017), 160–166.
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35
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35 Sluchanko, N.N., Klementiev, K.E., Shirshin, E.A., Tsoraev, G.V., Friedrich, T., Maksimov, E.G., The purple Trp288Ala mutant of Synechocystis OCP persistently quenches phycobilisome fluorescence and tightly interacts with FRP. Biochim. Biophys. Acta (BBA) Bioenerg. 1858 (2017), 1–11.
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36 Bonente, G., Howes, B.D., Caffarri, S., Smulevich, G., Bassi, R., Interactions between the photosystem II subunit PsbS and xanthophylls studied in vivo and in vitro. J. Biol. Chem. 283 (2008), 8434–8445.
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