The tetracycline resistance protein Tet(○) perturbs the conformation of the ribosomal decoding centre
Open accessAbstract
Summary: Tet(○) is an elongation factor‐like protein found in clinical isolates of Campylobacter jejuni that confers resistance to the protein‐synthesis inhibitor tetracycline. Tet(○) interacts with the 70S ribosome and promotes the release of bound tetracycline, however, as shown here, it does not form the same functional interaction with the 30S subunit. Chemical probing demonstrates that Tet(○) changes the reactivity of the 16S rRNA to dimethyl sulphate (DMS). These changes cluster within the decoding site, where C1214 is protected and A1408 is enhanced to DMS reactivity. C1214 is close to, but does not overlap, the primary tetracycline‐binding site, whereas A1408 is in a region distinct from the Tet(○) binding site visualized by cryo‐EM, indicating that Tet(○) induces long‐range rearrangements that may mediate tetracycline resistance. Tetracycline enhances C1054 to DMS modification but this enhancement is inhibited in the presence of Tet(○) unlike the tetracycline‐dependent protection of A892 which is unaffected by Tet(○). C1054 is part of the primary binding site of tetracycline and A892 is part of the secondary binding site. Therefore, the results for the first time demonstrate that the primary tetracycline binding site is correlated with tetracycline's inhibitory effect on protein synthesis.
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The 438-loop is not involved in interactions with Tc and is located about 15 Å away from Tc, but residue 437 is located in the near vicinity of nucleotides 1492-1493 in the 16S rRNA.
“Unlike the 507-loop, the 438-loop is not involved in the interactions with Tc, located about 15 Å away from Tc, but residue 437 is located in the near vicinity of nucleotides 1492–1493 in the 16S rRNA, where the decoding interaction network is observed in a normal translation ribosome 21.”
From Mechanism of tetracycline resistance by ribosomal protection protein Tet(O) (2013) · cites this paper as [21]
The bases of nucleotides 1492-1493 in the 16S rRNA flip out toward the Tet(O) 438-loop; this flipped-out conformation was also observed when codon-anticodon recognition takes place in a translating ribosome.
“In addition, the bases of nts 1492–1493 in the 16S rRNA flip out toward the Tet(O)’s 438-loop (Fig. 3); the flipped-out conformation that was also observed when a codon-anticodon recognition takes place in a translating ribosome 21.”
From Mechanism of tetracycline resistance by ribosomal protection protein Tet(O) (2013) · cites this paper as [21]
Tet(O) chases tetracyclines from the primary binding site but not the secondary binding site.
“(vi) Tet(O), an RPP which confers resistance to tetracycline, chases tetracyclines from the primary binding site but not the secondary binding site (12).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [12]
Protection of C1214 from DMS modification indicates that this base is directly shielded by Tet(O), supported by cryo-EM.
“The protection of C1214 from DMS modification would indicate that this base is directly shielded by Tet(O), and this conclusion is supported by the fact that the Tet(O) binding site observed by cryo-EM approaches C1214 (Fig. 4B).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [12]
On the 30S subunit, DMS probing localized Tet(O) interaction sites to h34 (C1214) and h44 (A1408), near the decoding site and the primary tetracycline-binding site.
“On the 30S subunit, sites of interaction were localized to h34 (C1214) and h44 (A1408), near the decoding site and the primary tetracycline-binding site (Fig. 4).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [12]
Tet(O) invokes structural rearrangements in h44.
“In addition to the proposed conformational change in h34 that results in tetracycline release, Tet(O) invokes structural rearrangements in h44 (12), a site distinct from both the primary tetracycline binding site (4, 37) and the Tet(O) binding site observed in the cryo-EM reconstruction (45).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [12]
A direct interaction between Tet(O) and tetracycline bound to the primary site cannot be absolutely discounted, although chemical probing and cryo-EM suggest it is not the case.
“It should be noted, however, that a direct interaction between Tet(O) and tetracycline bound to the primary site cannot be absolutely discounted, although both chemical probing and cryo-EM suggest this is not the case (12, 45).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [12]
Tet(O) specifically triggers the release of tetracycline from the primary tetracycline binding site.
“DMS-probing experiments showed that Tet(O) specifically triggers the release of tetracycline from the primary tetracycline binding site (12).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [12]
When biochemical and structural data describing the RPP's ribosomal binding site are combined, the interaction of the RPP with the ribosome can be modeled with high precision.
“When the biochemical (11, 12, 15) and structural (45) data describing the RPP's ribosomal binding site are combined, the interaction of the RPP with the ribosome can be modeled with high precision (Table 1).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [12]
The flipped-out conformation of A1492 and A1493 remains after the ribosome protection protein has left the ribosome.
“The enhancement of A1408 is also observed when TetO is bound with GTP rather than GDPNP (15), suggesting that the flipped-out conformation of A1492 and A1493 remains after the RPP has left the ribosome.”
From Structural basis for TetM-mediated tetracycline resistance (2012) · cites this paper as [15]
Additional density in the TetM•70S map fuses directly with C1054 of the 16S rRNA, a component of the primary tetracycline binding site.
“This additional density in the TetM•70S map fuses directly with C1054 of the 16S rRNA, a component of the primary tetracycline binding site (2, 3), and is consistent with the protection of C1054 from DMS modification observed upon TetO binding to the ribosome (15).”
From Structural basis for TetM-mediated tetracycline resistance (2012) · cites this paper as [15]
Binding of TetO to the ribosome leads to protection of C1214 and to a lesser extent C1054 within h34 from chemical modification, whereas the reactivity of A1408 in h44 is enhanced.
“Binding of TetO to the ribosome leads to protection of C1214 and to a lesser extent C1054 within h34 from chemical modification, whereas the reactivity of A1408 in h44 is enhanced (15).”
From Structural basis for TetM-mediated tetracycline resistance (2012) · cites this paper as [15]
TetO was suggested to chase tetracycline from the ribosome indirectly via inducing local disturbances within h34.
“As TetO is not observed to directly interact with C1054 or A1408 (14), TetO was suggested to chase tetracycline from the ribosome indirectly via inducing local disturbances within h34 (9,14,15).”
From Structural basis for TetM-mediated tetracycline resistance (2012) · cites this paper as [15]
TetM dislodges tetracycline from its binding site on the ribosome by disrupting the reported stacking interaction between the aromatic ring D of tetracycline and the nucleobase of C1054.
“This suggests that TetM dislodges tetracycline from its binding site on the ribosome by disrupting the reported stacking interaction between the aromatic ring D of tetracycline and the nucleobase of C1054 (2), in agreement with a previous proposal (15).”
From Structural basis for TetM-mediated tetracycline resistance (2012) · cites this paper as [15]
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Interplay of the ribosome A and CAR sites
Raval, M., Zhou, Y., Lynch, M., Krizanc, D., Thayer, K. M., & Weir, M. P. (2026) · NAR Genomics and Bioinformatics · doi:10.1093/nargab/lqag055 · Cited by 1 · see citing works
Resistance of Gram-negative Bacilli to Antimicrobials
Dean, C. R., Pascale, G. D., & Benton, B. M. (2018) · Springer eBooks · doi:10.1007/978-3-319-78538-7_4 · Cited by 1 · see citing works
Hannula, M. (2010) · Työväentutkimus Vuosikirja · Cited by 1 · see citing works
Inhibitors of the Elongation Cycle of Protein Synthesis
Wilson, D. N., Starosta, A. L., Yamamoto, H., & Nierhaus, K. H. (2009) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0000550.pub2
Self-citationBiosensors Micro and Nano Integration
Doraiswami, R. (2007) · Springer eBooks · doi:10.1007/978-0-387-46283-7_11
Functional insights into ABC-F proteins that mediate antibiotic resistance in Gram-positive bacteria
Sharkey, L. K. R. (2015) · White Rose eTheses Online (University of Leeds, The University of Sheffield, University of York)
Investigation of the Kinetics of Tet(O)-mediated Tetracycline Resistance
Li, J. (2010) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r3fd69
- Authors
- Connell, S. R., Trieber, C. A., Stelzl, U., Einfeldt, E., Taylor, D. E., & Nierhaus, K. H.
- Affiliations
- University of Alberta (CA)
- Max Planck Institute for Molecular Genetics (DE)
- Corresponding author
- Connell, Sean R.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2002-09
- Volume
- 45
- Issue
- 6
- Pages
- 1463-1472
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W1692011572
- Cited by
- 42
- References
- 46
- Citations by year
- 2026: 1 · 2023: 1 · 2022: 1 · 2020: 1 · 2019: 1 · 2018: 2 · 2016: 1 · 2015: 4 · 2014: 4 · 2013: 1 · 2012: 2
- FWCI
- 0.93
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- Alberta Heritage Foundation for Medical Research
- Natural Sciences and Engineering Research Council of Canada
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Medicine › Antibiotic Resistance in Bacteria
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- tetracycline resistance, Campylobacter jejuni, 16S rRNA, 30S ribosomal subunit, protein synthesis inhibition
- MeSH terms
- Bacterial Proteins, Binding Sites, Carrier Proteins, Models, Molecular, Molecular Conformation, Ribosomes, RNA, Ribosomal, 16S, Tetracycline Resistance, Protein Biosynthesis, Campylobacter jejuni
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