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      Revisiting the photosystem II repair cycle

      review-article
      Author(s): ,
      Publication date (Electronic):
      Journal: Plant Signaling & Behavior
      Publisher: Taylor & Francis
      Keywords: Chloroplast, D1, photosynthesis, photodamage, thylakoid membrane

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          ABSTRACT

          The ability of photosystem (PS) II to catalyze the light-driven oxidation of water comes along with its vulnerability to oxidative damage, in particular of the D1 core subunit. Photodamaged PSII undergoes repair in a multi-step process involving (i) reversible phosphorylation of PSII core subunits; (ii) monomerization and lateral migration of the PSII core from grana to stroma thylakoids; (iii) partial disassembly of PSII; (iv) proteolytic degradation of damaged D1; (v) replacement of damaged D1 protein with a new copy; (vi) reassembly of PSII monomers and migration back to grana thylakoids for dimerization and supercomplex assembly. Here we review the current knowledge on the PSII repair cycle.

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          Photosystem II assembly: from cyanobacteria to plants.

          Jörg Nickelsen, Birgit Rengstl (2012)
          Photosystem II (PSII) is an integral-membrane, multisubunit complex that initiates electron flow in oxygenic photosynthesis. The biogenesis of this complex machine involves the concerted assembly of at least 20 different polypeptides as well as the incorporation of a variety of inorganic and organic cofactors. Many factors have recently been identified that constitute an integrative network mediating the stepwise assembly of PSII components. One recurring theme is the subcellular organization of the assembly process in specialized membranes that form distinct biogenesis centers. Here, we review our current knowledge of the molecular components and events involved in PSII assembly and their high degree of evolutionary conservation.
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            Photosystem II core phosphorylation and photosynthetic acclimation require two different protein kinases.

            Kathryn Wagner, Paolo Pesaresi, Thomas Becker … (2005)
            Illumination changes elicit modifications of thylakoid proteins and reorganization of the photosynthetic machinery. This involves, in the short term, phosphorylation of photosystem II (PSII) and light-harvesting (LHCII) proteins. PSII phosphorylation is thought to be relevant for PSII turnover, whereas LHCII phosphorylation is associated with the relocation of LHCII and the redistribution of excitation energy (state transitions) between photosystems. In the long term, imbalances in energy distribution between photosystems are counteracted by adjusting photosystem stoichiometry. In the green alga Chlamydomonas and the plant Arabidopsis, state transitions require the orthologous protein kinases STT7 and STN7, respectively. Here we show that in Arabidopsis a second protein kinase, STN8, is required for the quantitative phosphorylation of PSII core proteins. However, PSII activity under high-intensity light is affected only slightly in stn8 mutants, and D1 turnover is indistinguishable from the wild type, implying that reversible protein phosphorylation is not essential for PSII repair. Acclimation to changes in light quality is defective in stn7 but not in stn8 mutants, indicating that short-term and long-term photosynthetic adaptations are coupled. Therefore the phosphorylation of LHCII, or of an unknown substrate of STN7, is also crucial for the control of photosynthetic gene expression.
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              Production of reactive oxygen species by photosystem II.

              Pavel Pospíšil (2009)
              Photosysthetic cleavage of water molecules to molecular oxygen is a crucial process for all aerobic life on the Earth. Light-driven oxidation of water occurs in photosystem II (PSII) - a pigment-protein complex embedded in the thylakoid membrane of plants, algae and cyanobacteria. Electron transport across the thylakoid membrane terminated by NADPH and ATP formation is inadvertently coupled with the formation of reactive oxygen species (ROS). Reactive oxygen species are mainly produced by photosystem I; however, under certain circumstances, PSII contributes to the overall formation of ROS in the thylakoid membrane. Under limitation of electron transport reaction between both photosystems, photoreduction of molecular oxygen by the reducing side of PSII generates a superoxide anion radical, its dismutation to hydrogen peroxide and the subsequent formation of a hydroxyl radical terminates the overall process of ROS formation on the PSII electron acceptor side. On the PSII electron donor side, partial or complete inhibition of enzymatic activity of the water-splitting manganese complex is coupled with incomplete oxidation of water to hydrogen peroxide. The review points out the mechanistic aspects in the production of ROS on both the electron acceptor and electron donor side of PSII.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Plant Signal Behav
                Journal ID (iso-abbrev): Plant Signal Behav
                Journal ID (publisher-id): KPSB
                Journal ID (publisher-id): kpsb20
                Title: Plant Signaling & Behavior
                Publisher: Taylor & Francis
                ISSN (Print): 1559-2316
                ISSN (Electronic): 1559-2324
                Publication date Collection: 2016
                Publication date (Electronic): 5 August 2016
                Publication date PMC-release: 5 August 2016
                Volume: 11
                Issue: 9
                Electronic Location Identifier: e1218587
                Affiliations
                Molekulare Biotechnologie & Systembiologie, TU Kaiserslautern , Kaiserslautern, Germany
                Author notes
                CONTACT Michael Schroda schroda@ 123456bio.uni-kl.de Molekulare Biotechnologie & Systembiologie, TU Kaiserslautern , Paul-Ehrlich-Str. 70, 67663 Kaiserslautern, Germany
                Article
                Publisher ID: 1218587
                DOI: 10.1080/15592324.2016.1218587
                PMC ID: 5058467
                PubMed ID: 27494214
                SO-VID: b12a6317-8014-4f50-82a1-dcaac6af5a8d
                Copyright © © 2016 The Author(s). Published with license by Taylor & Francis Group, LLC
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License http://creativecommons.org/licenses/by-nc/3.0/, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

                History
                Date received : 18 May 2016
                Date revision received : 23 July 2016
                Date accepted : 25 July 2016
                Page count
                Figures: 1, Tables: 0, References: 106, Pages: 8
                Categories
                Subject: Review

                ScienceOpen disciplines: Plant science & Botany
                Keywords: chloroplast,d1,photosynthesis,photodamage,thylakoid membrane
                Data availability:
                ScienceOpen disciplines: Plant science & Botany
                Keywords: chloroplast, d1, photosynthesis, photodamage, thylakoid membrane

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