Regulation of photosynthetic electron flow on dark to light transition by ferredoxin:NADP(H) oxidoreductase interactions
| Autor: | Manuela Kramer, Manuel Twachtmann, Melvin Rodriguez-Heredia, Laura Mosebach, Guy Hanke, Giovanni Finazzi, Anja Krieger-Liszkay, Francesco Saccon, Christopher D. P. Duffy, Robert J. Knell |
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| Přispěvatelé: | School of Biochemistry and Chemistry, Queen Mary University of London, Westfälische Wilhelms-Universität Münster = University of Münster (WWU), Universität Osnabrück - Osnabrück University, Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Light Photosynthesis & Metabolism (Photosynthesis), Physiologie cellulaire et végétale (LPCV), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Grenoble Alpes (UGA), Funding from the Deutsche Forschungsgemeinschaft through (Project 2 in the Collaborative Research Center (SFB) 944) and BBSRC (BB/R004838/1), Bayer Science and Education foundation (F-2016-BS-0555), ANR-10-LABX-0049,GRAL,Grenoble Alliance for Integrated Structural Cell Biology(2010), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017), ANR-10-LABX-0040,SPS,Saclay Plant Sciences(2010), ANR-10-INTB-1501,BioPol folders,Repliement et stabilisation par des polymeres amphiphiles biocompatibles de fragments scFv marqueurs cellulaires de cancers.(2010), European Project: 833184, ChloroMito, Institute for Plant Biology and Biotechnology,University of Münster, Department of Plant Physiology, University of Osnabrück |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0106 biological sciences
0301 basic medicine inorganic chemicals Chloroplasts QH301-705.5 Photoperiod Science thylakoid Arabidopsis Electrons Photosynthesis 01 natural sciences environment and public health General Biochemistry Genetics and Molecular Biology 03 medical and health sciences chloroplast Oxidoreductase NADPH [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology electron transport Biology (General) Ferredoxin chemistry.chemical_classification plant biology photosynthesis General Immunology and Microbiology biology Chemistry Arabidopsis Proteins General Neuroscience Biological Transport General Medicine Immunogold labelling biology.organism_classification ferredoxin Electron transport chain Chloroplast Ferredoxin-NADP Reductase 030104 developmental biology Thylakoid A. thaliana Biophysics Medicine bacteria 010606 plant biology & botany Research Article |
| Zdroj: | eLife eLife, 2021, 10, ⟨10.7554/eLife.56088⟩ eLife, eLife Sciences Publication, 2021, 10, ⟨10.7554/eLife.56088⟩ eLife, Vol 10 (2021) |
| ISSN: | 2050-084X |
| DOI: | 10.7554/eLife.56088⟩ |
| Popis: | International audience; During photosynthesis, electron transport is necessary for carbon assimilation and must be regulated to minimize free radical damage. There is a longstanding controversy over the role of a critical enzyme in this process (ferredoxin:NADP(H) oxidoreductase, or FNR), and in particular its location within chloroplasts. Here we use immunogold labelling to prove that FNR previously assigned as soluble is in fact membrane associated. We combined this technique with a genetic approach in the model plant Arabidopsis to show that the distribution of this enzyme between different membrane regions depends on its interaction with specific tether proteins. We further demonstrate a correlation between the interaction of FNR with different proteins and the activity of alternative photosynthetic electron transport pathways. This supports a role for FNR location in regulating photosynthetic electron flow during the transition from dark to light. |
| Databáze: | OpenAIRE |
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