1. Characterization of the putative iron sulfur protein IdiC (ORF5) in Synechococcus elongatus PCC 7942
- Author
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Daniel Pietsch, Klaus-Peter Michel, Dorothee Staiger, and Elfriede K. Pistorius
- Subjects
Iron-Sulfur Proteins ,Photosynthetic reaction centre ,iron limitation ,Protein subunit ,Molecular Sequence Data ,Mutant ,IdiC ,Plant Science ,Biology ,Photosystem I ,Biochemistry ,Antibodies ,Electron Transport ,Oxidoreductase ,photosynthetic ,Synechococcus elongatus PCC 7942 ,parasitic diseases ,Escherichia coli ,Amino Acid Sequence ,and respiratory electron transport chain ,oxidoreductase ,Ferredoxin ,Synechococcus ,chemistry.chemical_classification ,Sequence Homology, Amino Acid ,NDH-1 complex ,Wild type ,Computational Biology ,Gene Expression Regulation, Bacterial ,Cell Biology ,General Medicine ,ferredoxin ,chemistry ,Mutation ,NADP(+) ,Thioredoxin ,Sequence Alignment ,Genome, Bacterial - Abstract
The IdiC protein ((i) under bar ron (d) under bar eficiency (i) under bar nduced protein (C) under bar) is encoded by orf5 (now called idiC), which is part of the iron-responsive idiB operon of Synechococcus elongatus PCC 7942. The 20.5 kDa IdiC protein has a putative transmembrane helix and belongs to the thioredoxin (TRX)-like [2Fe-2S] ferredoxin family. IdiC has the highest similarity to the peripheral subunit NuoE of the Escherichia coli NDH-1 complex. IdiC expression increased under iron starvation and also in the late growth phase, representing growth conditions, which favor photosynthetic cyclic and respiratory electron transport over photosynthetic linear electron transport from water to NADP(+). Attempts to insertionally inactivate the idiC gene generated merodiploid mutants with a strongly reduced IdiC content (mutant MuD) but no IdiC-free mutant. Thus, IdiC seems to be an essential protein for the viability of S. elongatus under the used experimental conditions. Comparative analyses of S. elongatus wild type (WT) and mutant MuD showed that under iron limitation in WT and MuD the amount of the reaction center proteins PsbA and PsaA/B was highly reduced. MuD had a lower growth rate, chlorophyll content, and photosynthetic O-2 evolving activity with bicarbonate as electron acceptor than WT. Immunoblot analyses also showed that in MuD, when grown under iron limitation, the amount of the proteins IdiC and IdiB was greatly reduced as compared to WT. As a consequence of the reduction of the transcription factor IdiB, IdiA and IrpA expression were also decreased. In addition, the IsiA protein concentration was lower in MuD than in WT, although the isiA mRNA was equally high in MuD and WT. Another significant difference was the lower expression of the ferredoxin:NADP(+) oxidoreductase in mutant MuD under iron limitation compared to WT. A possible function of the protein IdiC in cyclic electron transport around photosystem I and/or in respiratory electron transport will be discussed.
- Published
- 2007
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