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Tetracyclines induce changes in accessibility of ribosomal proteins to proteases
I V Kolesnikov1, N Y Protasova, A T Gudkov
1Institute of Protein Research, Russian Academy of Sciences, Moscow Region, Russia.
Abstract:
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.
Insights
Tetracyclines bind to bacterial ribosomes, altering protein structure and function. This interaction influences antibiotic efficacy and antibiotic-binding sites near the peptidyl transferase center.
Area of Science:
- Molecular Biology
- Biochemistry
- Microbiology
Background:
- Tetracyclines are crucial antibiotics targeting bacterial protein synthesis.
- Ribosomes are the molecular machines responsible for translation.
- Understanding antibiotic-ribosome interactions is key to combating resistance.
Purpose of the Study:
- To investigate the interaction between tetracyclines and bacterial ribosomes.
- To identify how tetracycline binding affects ribosomal protein structure and accessibility.
- To map potential antibiotic-binding regions on the ribosome.
Main Methods:
- Limited proteolysis was employed to probe ribosomal protein structure.
- Free and tetracycline-bound ribosomes were compared using proteolysis.
- Protease susceptibility of ribosomal proteins was analyzed.
Main Results:
- Tetracycline binding alters the susceptibility of ribosomal proteins to proteases.
- Specific ribosomal proteins in the 30S and 50S subunits are affected.
- Affected proteins are primarily located on the 30S head and 50S interface.
Conclusions:
- Tetracycline interaction with ribosomes is dependent on antibiotic structure.
- A binding site for tetracyclines is proposed to be near the peptidyl transferase center.
- Conformational changes induced by tetracyclines may impact the translation process.