ИСТИНА

The DNA mismatch repair system occupies an important role in the life of a cell. Despite numerous works in this area, the biochemistry of the process remains not fully understood. It is known that the MutL, MutS, MutH proteins play a key role in the repair. In addition, sliding clamp proteins have also been shown to influence the speed and efficiency of the process. However, the direct interaction of these proteins has not yet been shown either in silico or in vivo. In this work, we applied an approach to the folding of proteins of the repair system and studied possible protein-protein interactions based on the Alphafold2 algorithm [1] and the FFT method. We have folded quaternary structures of proteins of the repair system (MutL, MutS, DNA sliding clamp) for bacteria Neisseria gonorrhoeae based on the amino acid sequences of the database. We chose the gonorrhea bacterium model, firstly, due to the relevance of the disease research topic [2], and secondly, because the study of the mismatch repair system in prokaryotes is less studied than for eukaryotes. Based on the quaternary structures, possible complexes were folded by the Alphafold2 and FFT methods with each other and with DNA fragments. Relationships between the obtained structures (calculated complexes) and experimental data are analyzed, the relationships and differences between the obtained structures and the known complexes of the repair system from the database of protein structures are shown.