Accepted_test

The transition of bacterial cells to a starved state under stress is accompanied by a significant decrease in their sensitivity to antibiotics, antiseptics, disinfectants and preservatives, which creates significant problems in the field of antibacterial measures for medicine and industries where sterility conditions are required. Ferritin-like DNA-binding proteins Dps and homologues play an important role in preserving the genetic material of bacteria in such conditions. The purpose of this work was to determine the prevalence of these proteins among bacteria, including pathogenic ones, and to study the possibilities of their DNA binding in a number of bacteria.

In this work, a number of DNA-binding ferritin-like bacterial proteins Dps were studied using molecular modeling and bioinformatics methods. The alignment of the primary sequences indicates high conservation of the iron-binding centers and a wide variety of lengths as well as sequences of the terminal regions. It has been shown that proteins capable of binding DNA are found in both gram-positive and gram-negative bacteria. The main influence on the ability to bind DNA is exerted by the surface charge of the protein and the presence of long (about 10-20 amino acid residues) free termini, which are embedded in DNA grooves and pull the DNA to the protein surface.