Tetracyclines induce changes in accessibility of ribosomal proteins to proteases.
Limited proteolysis was used to test the interaction of tetracyclines and some of their derivatives with ribosomes. Proteolysis of the free ribosomes was compared with that of the ligand-bound ribosomes. The interaction of different tetracyclines with ribosomes depends on their chemical structure and produces both a protective effect and an increased susceptibility to proteases of some ribosomal proteins in the 30S and 50S subparticles. Most of the proteins affected by tetracycline action are located on the head of the 30S and interface side of the 50S subunits. On the grounds of the obtained data one of the antibiotic-binding regions can be located near the ribosomal peptidyl transferase center. The effect of possible conformational changes induced by tetracyclines on the translation process is discussed.
Kolesnikov
I V
IV
Institute of Protein Research, Russian Academy of Sciences, Moscow Region, Russia.
Protasova
N Y
NY
Gudkov
A T
AT
D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D010450:Endopeptidases / Q000378:metabolism*; D008024:Ligands; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors / Q000378:metabolism; D012269:Ribosomal Proteins / Q000187:drug effects* / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism; D013752:Tetracycline / Q000737:chemistry / Q000494:pharmacology*
D000900:Anti-Bacterial Agents; D008024:Ligands; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D012269:Ribosomal Proteins; D010450:Endopeptidases; D013752:Tetracycline