Identification of OmpR-family response regulators interacting with thioredoxin in the Cyanobacterium Synechocystis sp. PCC 6803

PloS One
Taro KadowakiYukako Hihara

Abstract

The redox state of the photosynthetic electron transport chain is known to act as a signal to regulate the transcription of key genes involved in the acclimation responses to environmental changes. We hypothesized that the protein thioredoxin (Trx) acts as a mediator connecting the redox state of the photosynthetic electron transport chain and transcriptional regulation, and established a screening system to identify transcription factors (TFs) that interact with Trx. His-tagged TFs and S-tagged mutated form of Trx, TrxMC35S, whose active site cysteine 35 was substituted with serine to trap the target interacting protein, were co-expressed in E. coli cells and Trx-TF complexes were detected by immuno-blotting analysis. We examined the interaction between Trx and ten OmpR family TFs encoded in the chromosome of the cyanobacterium Synechocystis sp. PCC 6803 (S.6803). Although there is a highly conserved cysteine residue in the receiver domain of all OmpR family TFs, only three, RpaA (Slr0115), RpaB (Slr0947) and ManR (Slr1837), were identified as putative Trx targets [corrected].The recombinant forms of wild-type TrxM, RpaA, RpaB and ManR proteins from S.6803 were purified following over-expression in E. coli and their interactio...Continue Reading

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Citations

Nov 10, 2015·Biochimica Et Biophysica Acta·Annegret Wilde, Yukako Hihara
Aug 14, 2018·Plant & Cell Physiology·Frédéric DeschoenmaekerToru Hisabori

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Methods Mentioned

BETA
pull-down
PCR
electrophoresis
Protein Assay

Software Mentioned

CLUSTAL W

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