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Comparative Analysis of the Effect of Aminoglycosides on Bacterial Protein Synthesis in vitro
Open accessAbstract
The effect of aminoglycoside antibiotics on bacterial protein synthesis in an initiating system was investigated. Three classes of compounds can be differentiated as to their response. (1) Antibiotics (streptomycin, bluensomycin and hygromycin B) which inhibit polypeptide synthesis in a monophasic way indicating a single major inhibitory site. Polypeptides made under partially inhibitory conditions possess the same size as those produced without the drug. (2) Compounds containing 2‐deoxystreptamine in a diglycosylated form (gentamicins B, C 1, C 1a and C 2; sisomicin; kanamycin; neomycin; tobramycin; lividomycin A and paromomycin) inhibit protein synthesis in the triphasic way recently reported for gentamicin C complex which indicates multiple interactions of these antibiotics with the ribosome. These compounds also share the property of promoting the synthesis of longer than normal peptides due to termination errors. (3) The disaccharidic sisomicin and lividomycin cleavage products, garamine and lividamine respectively, give a biphasic response, namely stimulation of the rate of polypeptide synthesis at low concentration and inhibition at increasing concentrations. Aminoglycosides of class 2 (when present at second‐phase concentration) can revert the inhibition of protein synthesis caused by each of the class 1 compounds. Concomitantly, ‘read‐through’ products are accumulated.
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“HygB has a single binding site within the 30S (Figure 1) consistent with the finding that it has a monophasic effect on translation (Zierhut et al. 1979”
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 Zierhut et al. 1979
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“HygB has a monophasic effect on translation that is indicative of a single binding site on the ribosome (Zierhut et al. 1979”
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 Zierhut et al. 1979
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Research works printed but not linked: 24
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- 10.1111/j.1432-1033.1978.tb12347.x · DOI
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- 10.1073/pnas.75.11.5534 · DOI
- Weber K., 1975, RNA Phages, 51
- 10.1073/pnas.51.5.883 · DOI
- Gorini L., 1974, Ribosomes, 791
- 10.1073/pnas.61.2.768 · DOI
- 10.1073/pnas.67.3.1148 · DOI
- 10.7164/antibiotics.25.212 · DOI
- Davies J., 1965, Mol. Pharmacol., 1, 93
- Gale E. F., 1972, The Molecular Basis of Antibiotic Action, 278
Cited by
Sorted by citations
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
“…to render it inactive, or mimic the structure and function of the elongation factors and are thus able to a single binding site on the ribosome (Zierhut et al., 1979) and has been shown to bind close to the A site release the bound antibiotic from the ribosome (Mana-vathu et al., 1990;…”
Background
Metadata
- Authors
- ZIERHUT, G., PIEPERSBERG, W., & BÖCK, A.
- Affiliations
- University of Regensburg (DE)
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1979-08
- Volume
- 98
- Issue
- 2
- Pages
- 577-583
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W2074829556
- Cited by
- 35
- References
- 0
- Citations by year
- 2025: 1 · 2024: 1 · 2021: 1 · 2019: 1
- FWCI
- 0.69
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- European Journal of Biochemistry (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
- Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Microbial Natural Products and Biosynthesis
- Keywords
- aminoglycosides, bacterial protein synthesis, ribosome, streptomycin, hygromycin B, gentamicin, sisomicin, kanamycin, neomycin, tobramycin, paromomycin, 2-deoxystreptamine, readthrough, antibiotic binding sites
- MeSH terms
- Aminoglycosides, Bacterial Proteins, Drug Resistance, Microbial, Escherichia coli, Gentamicins, Kinetics, Ribosomes, Streptomycin, Structure-Activity Relationship, Protein Biosynthesis
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- The paper
- ZIERHUT, G., PIEPERSBERG, W., & BÖCK, A. (1979). Comparative Analysis of the Effect of Aminoglycosides on Bacterial Protein Synthesis in vitro. European Journal of Biochemistry. https://doi.org/10.1111/j.1432-1033.1979.tb13219.x