Tetracyclines induce changes in accessibility of ribosomal proteins to proteases
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.
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Tetracycline has one primary and multiple secondary binding sites within the small subunit.
“Tc has one primary and multiple secondary binding sites within the small subunit (Epe et al. 1987; Kolesnikov et al. 1996”
From The Structural Basis for the Action of the Antibiotics Tetracycline, Pactamycin, and Hygromycin B on the 30S Ribosomal Subunit (2000) · cites this paper as Kolesnikov et al. 1996
Cites
Goldman, R. A., Hasan, T., Hall, C. C., Strycharz, W. A., & Cooperman, B. S. (1983) · Biochemistry · doi:10.1021/bi00271a020 · Cited by 134 · see citing works
Sanchez-Pescador, R., Brown, J. T., Roberts, M., & Urdea, M. S. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.3.1218 · Cited by 87 · see citing works
Epe, B., Woolley, P., & Hornig, H. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)81539-9 · Cited by 50 · see citing works
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Brodersen, D. E., Clemons, W. M., Carter, A. P., Morgan-Warren, R. J., Wimberly, B. T., & Ramakrishnan, V. (2000) · Cell · doi:10.1016/s0092-8674(00)00216-6 · Cited by 950 · see citing works
“…an increase in the affinity of the A site for aminoacyl-tRNA (Eustice and Wilhelm, 1984a). binding sites within the small subunit (Epe et al., 1987; Kolesnikov et al., 1996), but the relevance of the second-Here we report the three-dimensional structures of the 30S ribosomal subunit from Thermus…”
Background
- Authors
- Kolesnikov, I.
- Affiliations
- Russian Academy of Sciences (RU)
- Corresponding author
- Kolesnikov, I
- Venue
- Biochimie
- Publisher
- Elsevier BV
- Published
- 1996
- Volume
- 78
- Issue
- 10
- Pages
- 868-873
- ISSN
- 0037-9042 (ISSN-L)
- 0300-9084
- OpenAlex
- W2090173216
- Cited by
- 5
- References
- 3
- Citations by year
- 2014: 1
- FWCI
- 0.00
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimie (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Pharmacology › Microbial Natural Products and Biosynthesis
- Keywords
- tetracycline, ribosome, ribosomal proteins, limited proteolysis, antibiotic binding sites, 30S subunit, 50S subunit, peptidyl transferase center, ribosome conformational change, translation (biology)
- MeSH terms
- Anti-Bacterial Agents, Ligands, Peptide Elongation Factors, Endopeptidases, Ribosomal Proteins, Ribosomes, Tetracycline, Peptide Elongation Factor G
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