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Cyanobacterial photoprotection by the orange carotenoid protein

Nature Plants volume 2, Article number: 16180 (2016) Cite this article

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Abstract

In photosynthetic organisms, the production of dangerous oxygen species is stimulated under high irradiance. To cope with this stress, these organisms have evolved photoprotective mechanisms. One type of mechanism functions to decrease the energy arriving at the photochemical centres by increasing thermal dissipation at the level of antennae. In cyanobacteria, the trigger for this mechanism is the photoactivation of a soluble carotenoid protein, the orange carotenoid protein (OCP), which is a structurally and functionally modular protein. The inactive orange form (OCPo) is compact and globular, with the carotenoid spanning the effector and the regulatory domains. In the active red form (OCPr), the two domains are completely separated and the carotenoid has translocated entirely into the effector domain. The activated OCPr interacts with the phycobilisome (PBS), the cyanobacterial antenna, and induces excitation-energy quenching. A second protein, the fluorescence recovery protein (FRP), dislodges the active OCPr from the PBSs and accelerates its conversion to the inactive OCP.

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Figure 1: The structures of the OCPo, RCP (NTD) and FRP.
Figure 2: The Synechocystis sp. PCC 6803 PBS.
Figure 3: Working model of OCP-related NPQ.
Figure 4: Models of OCP binding to the PBSs.

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Acknowledgements

The authors thank M. Sutter for assistance in figure preparation. D.K. is supported by the Commissariat à l'Energie Atomique, the Centre National de la Recherche Scientifique, and the Agence Nationale de la Recherche (project CYANOPROTECT). D.K.'s work was also partially supported by EU networks INTRO2 and HARVEST. C.A.K. is supported by the Office of Science of the US Department of Energy DE-FG02-91ER20021 with infrastructure support from MSU AgBIO Research. The authors thank all of the students, collaborators and colleagues that were involved in the characterization of the structure and function of the OCP.

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Authors and Affiliations

  1. Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette, France

    Diana Kirilovsky

  2. Institut de Biologie et Technologies de Saclay (iBiTec-S), Commissariat à l'Energie Atomique (CEA), 91191, Gif-sur-Yvette, France

    Diana Kirilovsky

  3. MSU-DOE Plant Research Laboratory and Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, 48824, Michigan, USA

    Cheryl A. Kerfeld

  4. Department of Plant and Microbial Biology, University of California, Berkeley, 94720, California, USA

    Cheryl A. Kerfeld

  5. Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, 94720, California, USA

    Cheryl A. Kerfeld

  6. Berkeley Synthetic Biology Institute, Berkeley, 94720, California, USA

    Cheryl A. Kerfeld

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C.A.K. and D.K. wrote the article.

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Kirilovsky, D., Kerfeld, C. Cyanobacterial photoprotection by the orange carotenoid protein. Nature Plants 2, 16180 (2016). https://doi.org/10.1038/nplants.2016.180

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