Abstract
The DNA-binding protein Dps plays a key role in the formation of Dps–DNA crystalline arrays in living bacterial cells, which allows bacteria to survive under stress conditions and under the influence of various adverse factors. Such genome-protective mechanisms can lead to the emergence of bacterial resistance to antibiotics and other drugs. Elucidation of the fundamental biochemical, genetic, and structural basis of the resistance is of primary importance for the development of strategies for combating and preventing bacterial resistance, as well as the elaboration of innovative therapeutic approaches. Conformational characteristics of Dps and its N-terminal fragments responsible for the nature of interactions of this protein with DNA in solution were studied by small-angle scattering.
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