Interaction of antibiotics with A- and P-site-specific bases in 16S ribosomal RNA
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We have studied the interactions of the antibiotics apramycin, kasugamycin, myomycin, neamine and pactamycin with 16S rRNA by chemical probing of drug-ribosome complexes. Kasugamycin and pactamycin, which are believed to affect translational initiation, protect bases in common with P-site-bound tRNA. While kasugamycin protects A794 and G926, and causes enhanced reactivity of C795, pactamycin protects G693 and C795. All four of these bases were previously shown to be protected by P-site tRNA or by edeine, another P-site inhibitor. Apramycin and neamine, which both induce miscoding and inhibit translocation, protect A1408, G1419 and G1494, as was also found earlier for neomycin, gentamicin, kanamycin and paromomycin. A1408 and G1494 were previously shown to be protected by A-site tRNA. Surprisingly, myomycin fails to give strong protection of any bases in 16S rRNA, in spite of having an apparently identical target site and mode of action to streptomycin, which protects several bases in the 915 region. Instead, myomycin gives only weak protection of A1408. These results suggest that the binding site(s) of streptomycin and myomycin have yet to be identified.
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Binding of pactamycin protects the N1 and N7 atoms of G693 and N3 of C795 from attack by kethoxal and DMS, respectively.
“binding of Pct protects the N1 and N7 atoms of G693 as well as N3 of C795 from attack by kethoxal and DMS, respectively (Egebjerg and Garrett 1991; Woodcock et al. 1991”
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 Woodcock et al. 1991
The pactamycin interactions seen in the structure are in excellent agreement with biochemical protection experiments.
“These interactions are in excellent agreement with biochemical experiments showing that binding of Pct protects the N1 and N7 atoms of G693 as well as N3 of C795 from attack by kethoxal and DMS, respectively”
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 Woodcock et al. 1991
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Research works printed but not linked: 5
- Cundliffe,E. (1981) In Gale,E.F., Cundliffe,E.* Reynolds,P.E.. Richmond,M.H. and Waring,M.J. (eds), The Molecular Basis of Antibiotic Action. John Wiley and Sons, New York, pp. 402 -457.
- Cundliffe,E. (1990) In Hill,W.E., Dahlberg,A.E., Garrett,R.A., Moore,P.B., Schlessinger,D. and Warner,J.R. (eds), The Ribosome, Structure, Function & Evolution. American Society for Microbiology, Washington, DC, pp. 479-490.
- De Stasio,E.A., Goringer,H.U., Tapprich,W.E. and Dahlberg,A.E. (1988) In Tuite,M.F., Picard,M. and Bolotin-Fukuhara,M. (eds), Genetics of Translation: New Approaches. Springer-Verlag, pp. 17-42.
- Moazed,D. and Noller,H.F. (1991) Proc. Natl. Acad. Sci. USA, in press.
- Noller,H.F., Moazed,D., Stem,S., Powers,T., Allen,P.N., Robertson,J.M., Weiser,B. and Triman,K. (1990) In Hill,W.E., Dahlberg,A.E., Garrett,R.A., Moore,P.B., Schlessinger,D. and Warner,J.R. (eds), The Ribosome. Structure, Function & Evolution. American Society for Microbiology, Washington, DC, pp. 73-92.
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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
“Binding of HygB does not seem to induce any significant respectively (Egebjerg and Garrett, 1991; Woodcock et al., 1991).”
BackgroundCrystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3
Pioletti, M., Schlünzen, F., Harms, J., Zarivach, R., Glühmann, M., Avila, H., Bashan, A., Bartels, H., Auerbach, T., Jacobi, C., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.8.1829 · Cited by 527 · see citing works
The A-Z of bacterial translation inhibitors
Wilson, D. N. (2009) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409230903307311 · Cited by 322 · see citing works
- Authors
- Woodcock, J., Moazed, D., Cannon, M., Davies, J., & Noller, H. F.
- Affiliations
- King's College London (GB)
- Venue
- The EMBO Journal
- Published
- 1991-10-01
- Volume
- 10
- Issue
- 10
- Pages
- 3099-3103
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC453027
- OpenAlex
- W196443510
- Cited by
- 229
- References
- 0
- Citations by year
- 2025: 1 · 2024: 7 · 2023: 1 · 2022: 4 · 2021: 1 · 2020: 5 · 2019: 3 · 2018: 6 · 2017: 3 · 2016: 2 · 2015: 2 · 2014: 8 · 2013: 6 · 2012: 6
- FWCI
- 2.12
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Eli Lilly and Company
- Wellcome Trust
- Nuffield Foundation
- National Institutes of Health (GM-17129)
- National Cancer Institute
- National Institute of General Medical Sciences (GM-17129)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Keywords
- antibiotics, 16S rRNA, A-site, P site, translation initiation, kasugamycin, pactamycin, apramycin, neamine, streptomycin, A-site tRNA, P-site tRNA, chemical probing
- MeSH terms
- Aminoglycosides, Anti-Bacterial Agents, Autoradiography, Escherichia coli, Nebramycin, Neomycin, Nucleic Acid Conformation, Nucleic Acid Hybridization, RNA, Ribosomal, 16S
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