Recognition of Cognate Transfer RNA by the 30 S Ribosomal Subunit
Abstract
Crystal structures of the 30 S ribosomal subunit in complex with messenger RNA and cognate transfer RNA in the A site, both in the presence and absence of the antibiotic paromomycin, have been solved at between 3.1 and 3.3 angstroms resolution. Cognate transfer RNA (tRNA) binding induces global domain movements of the 30 S subunit and changes in the conformation of the universally conserved and essential bases A1492, A1493, and G530 of 16 S RNA. These bases interact intimately with the minor groove of the first two base pairs between the codon and anticodon, thus sensing Watson-Crick base-pairing geometry and discriminating against near-cognate tRNA. The third, or “wobble,” position of the codon is free to accommodate certain noncanonical base pairs. By partially inducing these structural changes, paromomycin facilitates binding of near-cognate tRNAs.
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Helix 69 of the 23S rRNA is positioned beyond a bonding distance from Tet(O); the closest point (nucleotide 1914) is about 6 Å away from Tet(O).
“Interestingly, helix 69 of the 23S rRNA, which was repeatedly found to be involved in the interactions with other ribosomal factors such as the EF-Tu-aminoacyl-tRNA complex and EF-G 12,19, is positioned beyond a bonding distance from Tet(O). The closest point (nucleotide 1914) is about 6 Å away from Tet(O).”
From Mechanism of tetracycline resistance by ribosomal protection protein Tet(O) (2013) · cites this paper as [19]
The interaction between S12 and Tet(O) at multiple sites is similar to the bridge-like connection that S12 forms with two sites of the A/T-site tRNA in the EF-Tu-tRNA complex.
“This interaction between S12 and Tet(O) at multiple sites is similar to the bridge-like connection that S12 forms with two sites of the A/T-site tRNA in the EF-Tu-tRNA complex, as previously described for the X-ray structure of the ternary complex-bound ribosome complex 19.”
From Mechanism of tetracycline resistance by ribosomal protection protein Tet(O) (2013) · cites this paper as [19]
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- Authors
- Ogle, J. M., Brodersen, D. E., Clemons, W. M., Tarry, M. J., Carter, A. P., & Ramakrishnan, V.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Ramakrishnan, V.
- Venue
- Science
- Published
- 2001-05-04
- Volume
- 292
- Issue
- 5518
- Pages
- 897-902
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2145583354
- Cited by
- 1,162
- References
- 49
- Citations by year
- 2026: 20 · 2025: 14 · 2024: 33 · 2023: 27 · 2022: 33 · 2021: 42 · 2020: 21 · 2019: 29 · 2018: 40 · 2017: 32 · 2016: 38 · 2015: 36 · 2014: 51 · 2013: 55 · 2012: 50
- FWCI
- 23.39
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- National Institutes of Health (5r01gm044973-14)
- National Institute of General Medical Sciences (GM 44973, F31GM019384)
- 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
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- 30S ribosomal subunit, codon-anticodon pairing, 16S rRNA, paromomycin, near-cognate tRNA, wobble position, tRNA binding, ribosome structure, antibiotic binding
- MeSH terms
- Anti-Bacterial Agents, Anticodon, Binding Sites, Codon, Guanosine Triphosphate, Hydrogen Bonding, Models, Molecular, Nucleic Acid Conformation, Paromomycin, Peptide Chain Elongation, Translational, Peptide Elongation Factor Tu, Ribosomes, RNA, Bacterial, RNA, Messenger, RNA, Ribosomal, 16S, RNA, Transfer, RNA, Transfer, Amino Acid-Specific, RNA, Transfer, Phe, Thermodynamics, Protein Biosynthesis, Thermus thermophilus, Crystallography, X-Ray, Base Pairing
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