Asst. Prof. Marko Močibob from the Department of Biochemistry, in collaboration with scientists from the Faculty of Pharmacy and Biochemistry, published an article entitled Ribosomal A site binding pattern differs between Arm methyltransferases from clinical pathogens and a natural producer of aminoglycosides in the International Journal of Biological Macromolecules (IF = 7.7).
In the aforementioned article, the authors deal with the problem of resistance to aminoglycoside antibiotics, mediated by 16S rRNA methyltransferases. Aminoglycoside antibiotics (e.g. streptomycin, kanamycin, gentamicin...) bind to the decoding site of the small subunit of the ribosome and interfere with the correct translation of mRNA and inhibit protein biosynthesis. 16S rRNA methyltransferases methylate the ribosomal RNA of the small subunit of the ribosome, thus preventing the binding and antibiotic action of aminoglycoside antibiotics. They are present in bacteria that naturally produce aminoglycosides, but have also been found in resistant strains of bacteria that cause hospital infections. In the published article, the properties and determinants of the binding of 16S rRNA methyltransferases from resistant clinical isolates and the bacterium Micromonospora zionensis, a natural producer of the aminoglycoside antibiotic 6-N-methyl-sisomycin, were compared. The published results indicate significant differences in the binding and methylation of rRNA between natural producers and resistant pathogenic strains, and open the possibility of developing antibiotics that will also work against pathogens resistant to existing aminoglycoside antibiotics.
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