Flavodiiron proteins Flv1 and Flv3 enable cyanobacterial growth and photosynthesis under fluctuating light
| Autor: | Natalia Battchikova, Yagut Allahverdiyeva, Ghada Ajlani, Eva-Mari Aro, Luca Bersanini, Laurent Cournac, Henna Mustila, Maria Ermakova, Pierre Richaud |
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| Přispěvatelé: | 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) |
| Rok vydání: | 2013 |
| Předmět: |
0106 biological sciences
Cyanobacteria photorespiration Light Flavodoxin ta1172 Biology Photosystem I Photosynthesis membrane inlet mass spectrometry 01 natural sciences 03 medical and health sciences Bacterial Proteins Oxidoreductase terminal oxidases 030304 developmental biology chemistry.chemical_classification 0303 health sciences Multidisciplinary Flavoproteins Synechocystis ta1182 Carbon Dioxide Biological Sciences biology.organism_classification Anabaena [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology Electron transport chain Oxygen Light intensity chemistry Biochemistry Mehler reaction Genes Bacterial Mutation biology.protein Protein Multimerization 010606 plant biology & botany |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, 2013, 110 (10), pp.4111-4116. ⟨10.1073/pnas.1221194110⟩ Proceedings of the National Academy of Sciences |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.1221194110 |
| Popis: | Cyanobacterial flavodiiron proteins (FDPs; A-type flavoprotein, Flv) comprise, besides the β-lactamase–like and flavodoxin domains typical for all FDPs, an extra NAD(P)H:flavin oxidoreductase module and thus differ from FDPs in other Bacteria and Archaea. Synechocystis sp. PCC 6803 has four genes encoding the FDPs. Flv1 and Flv3 function as an NAD(P)H:oxygen oxidoreductase, donating electrons directly to O 2 without production of reactive oxygen species. Here we show that the Flv1 and Flv3 proteins are crucial for cyanobacteria under fluctuating light, a typical light condition in aquatic environments. Under constant-light conditions, regardless of light intensity, the Flv1 and Flv3 proteins are dispensable. In contrast, under fluctuating light conditions, the growth and photosynthesis of the Δ flv1(A) and/or Δ flv3(A) mutants of Synechocystis sp. PCC 6803 and Anabaena sp. PCC 7120 become arrested, resulting in cell death in the most severe cases. This reaction is mainly caused by malfunction of photosystem I and oxidative damage induced by reactive oxygen species generated during abrupt short-term increases in light intensity. Unlike higher plants that lack the FDPs and use the Proton Gradient Regulation 5 to safeguard photosystem I, the cyanobacterial homolog of Proton Gradient Regulation 5 is shown not to be crucial for growth under fluctuating light. Instead, the unique Flv1/Flv3 heterodimer maintains the redox balance of the electron transfer chain in cyanobacteria and provides protection for photosystem I under fluctuating growth light. Evolution of unique cyanobacterial FDPs is discussed as a prerequisite for the development of oxygenic photosynthesis. |
| Databáze: | OpenAIRE |
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