Abstract
The universal response of Escherichia coli to stress is enhancing the synthesis of specific histone-like Dps proteins that bind bacterial DNA. As a result, two-dimensional and three-dimensional crystalline arrays can be observed in the cytoplasm of starving bacteria. Conditions for obtaining in vitro co-crystals of DNA-Dps were selected, and their elemental composition was studied using analytical electron microscopy. It was found that Dps in the co-crystal retains its ferritin-like activity; that is, it can stimulate the oxidation of Fe2+ ions to Fe3+ and facilitate the accumulation of iron in the form of Fe2O3 in the inner cavity of the oligomer.
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ACKNOWLEDGMENTS
Analytical electron and fluorescence microscopy were performed with the financial support from the Russian Science Foundation (project no. 19-74-30003). The expression and purification of the Dps protein was carried out as part of the state task of the Russian Ministry of Education and Science (topic 0082-2014-0001, no. AAAA-A17-117040610310-6, and topic 0104-2019-0005). The electron microscopy was carried out using a JEOL2100 analytical electron microscope (JEOL, Japan) as part of a unique research facility “Three-Dimensional Electron Microscopy and Spectroscopy” of the Faculty of Biology of Moscow State University.
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Moiseenko, A.V., Loiko, N.G., Chertkov, O.V. et al. Analysis of Element Composition of DNA-Protein Crystals In Vitro. Moscow Univ. Biol.Sci. Bull. 74, 240–245 (2019). https://doi.org/10.3103/S0096392519040102
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DOI: https://doi.org/10.3103/S0096392519040102