Morphological peculiarities of the DNA-protein complexes in starved Escherichia coli cells.

• Main Authors: Natalia Loiko, Yana Danilova, Andrey Moiseenko, Vladislav Kovalenko, Ksenia Tereshkina, Maria Tutukina, Galina El-Registan, Olga Sokolova, Yurii Krupyanskii
• Format: Article
• Language: English
• Published: Public Library of Science (PLoS) 2020-01-01
• Series: PLoS ONE
• Online Access: https://doi.org/10.1371/journal.pone.0231562

One of the adaptive strategies for the constantly changing conditions of the environment utilized in bacterial cells involves the condensation of DNA in complex with the DNA-binding protein, Dps. With the use of electron microscopy and electron tomography, we observed several morphologically different types of DNA condensation in dormant Escherichia coli cells, namely: nanocrystalline, liquid crystalline, and the folded nucleosome-like. We confirmed the presence of both Dps and DNA in all of the ordered structures using EDX analysis. The comparison of EDX spectra obtained for the three different ordered structures revealed that in nanocrystalline formation the majority of the Dps protein is tightly bound to nucleoid DNA. The dps-null cells contained only one type of condensed DNA structure, liquid crystalline, thus, differing from those with Dps. The results obtained here shed some light on the phenomenon of DNA condensation in dormant prokaryotic cells and on the general problem of developing a response to stress. We demonstrated that the population of dormant cells is structurally heterogeneous, allowing them to respond flexibly to environmental changes. It increases the ability of the whole bacterial population to survive under extreme stress conditions.