The bacterial-type [4Fe-4S] ferredoxin 7 has a regulatory function under photooxidative stress conditions in the cyanobacterium Synechocystis sp. PCC 6803.
Ferredoxins function as electron carrier in a wide range of metabolic and regulatory reactions. It is not clear yet, whether the multiplicity of ferredoxin proteins is also reflected in functional multiplicity in photosynthetic organisms. We addressed the biological function of the bacterial-type ferredoxin, Fed7 in the cyanobacterium Synechocystis sp. PCC 6803. The expression of fed7 is induced under low CO₂ conditions and further enhanced by additional high light treatment. These conditions are considered as promoting photooxidative stress, and prompted us to investigate the biological function of Fed7 under these conditions. Loss of Fed7 did not inhibit growth of the mutant strain Δfed7 but significantly modulated photosynthesis parameters when the mutant was grown under low CO₂ and high light conditions. Characteristics of the Δfed7 mutant included elevated chlorophyll and photosystem I levels as well as reduced abundance and activity of photosystem II. Transcriptional profiling of the mutant under low CO₂ conditions demonstrated changes in gene regulation of the carbon concentrating mechanism and photoprotective mechanisms such as the Flv2/4 electron valve, the PSII dimer stabilizing protein Sll0218, and chlorophyll biosynthesis. We conclude that the function of Fed7 is connected to coping with photooxidative stress, possibly by constituting a redox-responsive regulatory element in photoprotection. In photosynthetic eukaryotes domains homologous to Fed7 are exclusively found in chloroplast DnaJ-like proteins that are likely involved in remodeling of regulator protein complexes. It is conceivable that the regulatory function of Fed7 evolved in cyanobacteria and was recruited by Viridiplantae as the controller for the chloroplast DnaJ-like proteins.
Laboratory of Molecular Plant Biology, Department of Biochemistry, University of Turku, 20014 Turku, Finland. Electronic address: hmsile@utu.fi.
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Mustila
Laboratory of Molecular Plant Biology, Department of Biochemistry, University of Turku, 20014 Turku, Finland. Electronic address: allahve@utu.fi.
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Allahverdiyeva
Laboratory of Molecular Plant Biology, Department of Biochemistry, University of Turku, 20014 Turku, Finland. Electronic address: jaheis@utu.fi.
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Isojärvi
Laboratory of Molecular Plant Biology, Department of Biochemistry, University of Turku, 20014 Turku, Finland. Electronic address: evaaro@utu.fi.
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Aro
Laboratory of Molecular Plant Biology, Department of Biochemistry, University of Turku, 20014 Turku, Finland. Electronic address: m.eisenhut@hhu.de.
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Eisenhut
D002245:Carbon Dioxide / Q000378:metabolism; D002734:Chlorophyll / Q000378:metabolism; D002736:Chloroplasts / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D005288:Ferredoxins / Q000235:genetics* / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D050956:HSP40 Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008027:Light; D009154:Mutation; D018384:Oxidative Stress / Q000235:genetics*; D010788:Photosynthesis / Q000235:genetics*; D045331:Photosystem I Protein Complex / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D046939:Synechocystis / Q000235:genetics / Q000378:metabolism
D005288:Ferredoxins; D050956:HSP40 Heat-Shock Proteins; D045331:Photosystem I Protein Complex; D002734:Chlorophyll; D002245:Carbon Dioxide
Bacterial-type ferredoxin; Chloroplast DnaJ-like protein; Photooxidative stress; Regulation; Synechocystis