Effects of Tetracycline and Spectinomycin on the Tertiary Structure of Ribosomal RNA in the Escherichia coli 30 S Ribosomal Subunit
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Structural analysis of the 16 S rRNA in the 30 S subunit and 70 S ribosome in the presence of ribosome-specific antibiotics was performed to determine whether they produced rRNA structural changes that might provide further insight to their action. An UV cross-linking procedure that determines the pattern and frequency of intramolecular 16 S RNA cross-links was used to detect differences reflecting structural changes. Tetracycline and spectinomycin have specific effects detected by this assay. The presence of tetracycline inhibits the cross-link C967xC1400 completely, increases the frequency of cross-link C1402x1501 twofold, and decreases the cross-link G894xU244 by one-half without affecting other cross-links. Spectinomycin reduces the frequency of the cross-link C934xU1345 by 60% without affecting cross-linking at other sites. The structural changes occur at concentrations at which the antibiotics exert their inhibitory effects. For spectinomycin, the apparent binding site and the affected cross-linking site are distant in the secondary structure but are close in tertiary structure in several recent models, indicating a localized effect. For tetracycline, the apparent binding sites are significantly separated in both the secondary and the three-dimensional structures, suggesting a more regional effect.
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The UV-induced cross-link between C1402 and C1501 in H44 increases in intensity upon tetracycline binding.
“In addition, the UV-induced cross-link between C1402 and C1501, both of which are located in H44, increases in intensity upon Tc binding (Noah et al. 1999”
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 Noah et al. 1999
Tetracycline inhibits the UV-induced cross-link C967-C1400 completely, an interaction which links the H31 stem loop to the top of the functionally important H44.
“Tc is known to inhibit the UV-induced cross-link C967-C1400 completely (Figure 2A), an interaction which links the H31 stem loop to the top of the functionally important H44 (Noah et al. 1999”
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 Noah et al. 1999
A conformational change can be inferred from several biochemical experiments.
“a conformational change can be inferred from several biochemical experiments (11, 14, 32, 56).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [32]
A UV-dependent cross-link between C1402 and C1501 at the top of h44 is enhanced by the presence of tetracycline.
“They observed that a UV-dependent cross-link between C1402 and C1501, two bases located at the top of h44, is enhanced by the presence of tetracycline.”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [32]
The enhancement of the C1402-C1501 cross-link may indicate that tetracycline promotes subtle structural rearrangement or fixes the ribosome in a conformation favorable for the cross-link.
“These bases are distinct from the observed tetracycline binding sites and may indicate that tetracycline is promoting subtle structural rearrangement or fixing the ribosome in a conformation that is favorable for the establishment of the C1402-C1501 cross-link.”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [32]
Tetracycline affects h44.
“Noah et al. (32) presented evidence that tetracycline affects h44.”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [32]
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References 29 · Cited by 46
- Authors
- Noah, J. W., Dolan, M. A., Babin, P., & Wollenzien, P.
- Affiliations
- North Carolina State University (US)
- Corresponding author
- Wollenzien, Paul
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-06
- Volume
- 274
- Issue
- 23
- Pages
- 16576-16581
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1963836062
- Cited by
- 46
- References
- 29
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2020: 1 · 2019: 3 · 2018: 1 · 2017: 1 · 2016: 6 · 2014: 3
- FWCI
- 1.27
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM 43237, R01GM043237)
- 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 › DNA and Nucleic Acid Chemistry
- Keywords
- tetracycline, spectinomycin, 16S rRNA, 30S ribosomal subunit, Escherichia coli, antibiotic binding sites, UV crosslinking, RNA secondary structure, antibiotic mechanism of action
- MeSH terms
- Spectinomycin, Anti-Bacterial Agents, Base Sequence, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Models, Molecular, Molecular Sequence Data, Nucleic Acid Conformation, Ribosomes, RNA, Bacterial, RNA, Ribosomal, 16S, Tetracycline, Ultraviolet Rays
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