Tetracycline can inhibit tRNA binding to the ribosomal P site as well as to the A site
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A and P sites of Escherichia coli ribosomes were titrated with AcPhe‐tRNA Phe, in the absence or presence of tetracycline. The P‐site location of the bound AcPhe‐tRNA was assessed by means of a quantitative puromycin reaction. The results demonstrate that, in agreement with the generally held view, tetracycline exclusively inhibits the A‐site binding, if the statistical number of bound acyl‐tRNA molecules per ribosome does not exceed about 0.5. However, above this value the P site becomes sensitive to tetracycline as well. It follows that the tightly coupled 70S ribosomes used in functional studies appear to be functionally heterogeneous, i. e. those P sites which cannot be affected by tetracycline are preferentially occupied by AcPhe‐tRNA, whereas higher concentrations of this tRNA species are required to fill tetracycline‐sensitive P sites. Furthermore, the results imply that under tRNA saturation conditions the tetracycline inhibition cannot be used as an indicator for the site location of bound tRNA.
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Tetracyclines inhibit protein synthesis by blocking the binding of aminoacylated tRNA to the A site.
“where they inhibit protein synthesis by blocking the binding of aminoacylated tRNA (aa-tRNA) to the A site (Maxwell 1967; Geigenmuller and Nierhaus 1986”
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 Geigenmuller and Nierhaus 1986
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References 14 · Cited by 45
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- Cundliffe, E. (1980) in Ribosomes; Structure, function andgenetics (Chambliss, G., Craven, G. R., Davies, J., Davis, K., Kahan, L. & Nomura, M., eds) pp 555-581, University Park Press, Baltimore.
- Sarkar, S. & Thach, R. E. (1968) Proc. Natl Acad. Sci. U S A 60.
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- Rheinberger, H.-J. & Nierhaus, K. H. (1986) J. Biol. Chem. 261, 221 -228. 805 -809. USA 68,1474-1478. 9133-9139. 14321033, 1986, 3, Downloaded from https://febs.onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1986.tb10499.x, Wiley Online Library on [02/12/2023]. See the Terms and Conditions (https://onlinelibrary.wiley.com/terms-and-conditions) on Wiley Online Library for rules of use; OA articles are governed by the applicable Creative Commons License
- Authors
- GEIGENMÜLLER, U., & NIERHAUS, K. H.
- Affiliations
- Max Planck Institute for Molecular Genetics (DE)
- Corresponding author
- NIERHAUS, Knud H.
- ORCID
- GEIGENMÜLLER, Ute
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1986-12
- Volume
- 161
- Issue
- 3
- Pages
- 723-726
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W1989023859
- Cited by
- 45
- References
- 14
- Citations by year
- 2025: 1 · 2022: 1 · 2021: 1 · 2020: 1 · 2019: 2 · 2018: 2 · 2016: 3 · 2015: 1 · 2014: 1 · 2013: 1 · 2012: 1
- FWCI
- 0.86
- 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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Keywords
- tetracycline, ribosomal P site, ribosomal A site, tRNA binding, 70S ribosome, ribosome heterogeneity, Escherichia coli ribosome
- MeSH terms
- Allosteric Site, Binding Sites, Binding, Competitive, Models, Biological, Puromycin, Ribosomes, RNA, Transfer, RNA, Transfer, Amino Acyl, Tetracycline
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