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      Dynamic reorganization of photosynthetic supercomplexes during environmental acclimation of photosynthesis

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          Abstract

          Plants and algae have acquired the ability to acclimate to ever-changing environments in order to survive. During photosynthesis, light energy is converted by several membrane protein supercomplexes into electrochemical energy, which is eventually used to assimilate CO 2. The efficiency of photosynthesis is modulated by many environmental factors such as quality and quantity of light, temperature, drought, and CO 2 concentration, among others. Accumulating evidence indicates that photosynthetic supercomplexes undergo supramolecular reorganization within a short time frame during acclimation to an environmental change. This reorganization includes state transitions that balance the excitation of photosystem I and II by shuttling peripheral antenna proteins between the two, thermal energy dissipation that occurs at energy-quenching sites within the light-harvesting antenna generated for negative feedback when excess light is absorbed, and cyclic electron flow that is facilitated between photosystem I and the cytochrome bf complex when cells demand more ATP and/or need to activate energy dissipation. This review will highlight the recent findings regarding these environmental acclimation events in model organisms with particular attention to the unicellular green alga C. reinhardtii and with reference to the vascular plant A. thaliana, which offers a glimpse into the dynamic behavior of photosynthetic machineries in nature.

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          Photoprotection and Other Responses of Plants to High Light Stress

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            A pigment-binding protein essential for regulation of photosynthetic light harvesting.

            Photosynthetic light harvesting in plants is regulated in response to changes in incident light intensity. Absorption of light that exceeds a plant's capacity for fixation of CO2 results in thermal dissipation of excitation energy in the pigment antenna of photosystem II by a poorly understood mechanism. This regulatory process, termed nonphotochemical quenching, maintains the balance between dissipation and utilization of light energy to minimize generation of oxidizing molecules, thereby protecting the plant against photo-oxidative damage. To identify specific proteins that are involved in nonphotochemical quenching, we have isolated mutants of Arabidopsis thaliana that cannot dissipate excess absorbed light energy. Here we show that the gene encoding PsbS, an intrinsic chlorophyll-binding protein of photosystem II, is necessary for nonphotochemical quenching but not for efficient light harvesting and photosynthesis. These results indicate that PsbS may be the site for nonphotochemical quenching, a finding that has implications for the functional evolution of pigment-binding proteins.
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              REGULATION OF LIGHT HARVESTING IN GREEN PLANTS.

              When plants are exposed to light intensities in excess of those that can be utilized in photosynthetic electron transport, nonphotochemical dissipation of excitation energy is induced as a mechanism for photoprotection of photosystem II. The features of this process are reviewed, particularly with respect to the molecular mechanisms involved. It is shown how the dynamic properties of the proteins and pigments of the chlorophyll a/b light-harvesting complexes of photosystem II first enable the level of excitation energy to be sensed via the thylakoid proton gradient and subsequently allow excess energy to be dissipated as heat by formation of a nonphotochemical quencher. The nature of this quencher is discussed, together with a consideration of how the variation in capacity for energy dissipation depends on specific features of the composition of the light-harvesting system. Finally, the prospects for future progress in understanding the regulation of light harvesting are assessed.
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                Author and article information

                Journal
                Front Plant Sci
                Front Plant Sci
                Front. Plant Sci.
                Frontiers in Plant Science
                Frontiers Media S.A.
                1664-462X
                24 October 2013
                17 December 2013
                2013
                : 4
                : 513
                Affiliations
                Division of Environmental Photobiology, National Institute for Basic Biology Okazaki, Japan
                Author notes

                Edited by: Helmut Kirchhoff, Washington State University, USA

                Reviewed by: Jean-David Rochaix, University of Geneva, Switzerland; Krishna Niyogi, HHMI/University of California, USA

                *Correspondence: Jun Minagawa, Division of Environmental Photobiology, National Institute for Basic Biology, 38 Nishigonaka, Okazaki 444-8585, Japan e-mail: minagawa@ 123456nibb.ac.jp

                This article was submitted to Plant Physiology, a section of the journal Frontiers in Plant Science.

                Article
                10.3389/fpls.2013.00513
                3865443
                24381578
                821875d2-910b-49d8-aaf1-a42db71f8455
                Copyright © 2013 Minagawa.

                This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

                History
                : 18 September 2013
                : 30 November 2013
                Page count
                Figures: 4, Tables: 0, Equations: 0, References: 111, Pages: 11, Words: 9828
                Categories
                Plant Science
                Review Article

                Plant science & Botany
                acclimation,phosphorylation,electron transfer,light-harvesting complex,non-photochemical quenching

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