The role of iodine in plants remains poorly understood. Recent studies suggest that plants not only accumulate iodine, but also incorporate it into organic compounds, including proteins. The identification of plant-derived thyroid hormone analogs (T3 and T4) raises fundamental questions about the biosynthesis of these molecules and their potential physiological roles in plants.
In this study, we aimed to identify proteins from the Arabidopsis thaliana proteome, that could, based on their structural features, serve as potential scaffolds for the synthesis of T3 and T4 analogs. Using bioinformatic tools, we narrowed the candidate list to the following five proteins, suitable for recombinant expression in a bacterial system: Q9M8Z7, Q9C6Z3, Q501D5, F4J9A0 and O81888. The corresponding coding sequences were cloned into a selected expression vector, expressed in Escherichia coli and purified via nickel affinity chromatography.
Two proteins were expressed in bacteria, however, under the tested conditions, both localized to the insoluble fraction. To obtain sufficient quantities of soluble protein for further analysis, optimization of expression conditions would be required.
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