Binding Interaction between Tet(M) and the Ribosome: Requirements for Binding
Open accessAbstract
Tet(M) protein interacts with the protein biosynthesis machinery to render this process resistant to tetracycline by a mechanism which involves release of the antibiotic from the ribosome in a reaction dependent on GTP hydrolysis. To clarify this resistance mechanism further, the interaction of Tet(M) with the ribosome has been examined by using a gel filtration assay with radioactively labelled Tet(M) protein. The presence of GTP and 5′-guanylyl imido diphosphate, but not GDP, promoted Tet(M)-ribosome complex formation. Furthermore, thiostrepton, which inhibits the activities of elongation factor G (EF-G) and EF-Tu by binding to the ribosome, blocks stable Tet(M)-ribosome complex formation. Direct competition experiments show that Tet(M) and EF-G bind to overlapping sites on the ribosome.
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Tet(O) and EF-G bind to a common site located at the interface of the ribosomal subunit on the A site side, at the base of the L7/L12 stalk.
“Also evident in the reconstruction is that Tet(O) and EF-G are binding to a common site located at the interface of the ribosomal subunit on the A site side, at the base of the L7/L12 stalk (Fig. 3), in agreement with Dantley et al. (15).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [15]
The ribosome-binding site for RPPs was first localized to the elongation factor binding site when Dantley et al. showed that Tet(M) and EF-G compete for a similar site on the ribosome.
“The binding site was first localized to the elongation factor binding site when Dantley et al. (15) showed that Tet(M) and EF-G compete for a similar site on the ribosome.”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [15]
A component of the common Tet(M)/EF-G binding site is the L11 region on the 50S subunit.
“Additionally, the experiments of Dantley et al. (15) suggested that a component of this common site is the L11 region on the 50S subunit. This derives from the fact that the antibiotic thiostrepton, which binds this region and apparently locks in it a conformation unfavorable for EF-G binding (7), also inhibits the binding of Tet(M) (15).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [15]
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References 29 · Cited by 37
Research works printed but not linked: 1
- [1]Ausubel F M, Brent R, Kingston R E, Moore D D, Seidman J G, Smith J A, Struhl K. Current protocols in molecular biology. New York, N.Y: John Wiley & Sons, Inc.; 1987. [Google Scholar]
- Authors
- Dantley, K. A., Dannelly, H. K., & Burdett, V.
- Affiliations
- Duke University (US)
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 1998-08-15
- Volume
- 180
- Issue
- 16
- Pages
- 4089-4092
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC107402
- OpenAlex
- W1577886434
- Cited by
- 37
- References
- 29
- Citations by year
- 2026: 1 · 2022: 2 · 2021: 1 · 2019: 1 · 2018: 1 · 2017: 1 · 2015: 2 · 2014: 4 · 2012: 1
- FWCI
- 0.70
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Bacteriology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ai015619-18)
- National Institute of Allergy and Infectious Diseases (AI15619)
- 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 Medicine › Antibiotic Resistance in Bacteria
- Keywords
- tetracycline resistance, ribosome binding, GTP hydrolysis, thiostrepton, elongation factor G, elongation factor Tu, protein synthesis inhibition, binding site overlap
- MeSH terms
- Anti-Bacterial Agents, Bacterial Proteins, Binding Sites, Escherichia coli, Guanosine Triphosphate, Guanylyl Imidodiphosphate, Peptide Elongation Factors, Ribosomes, Tetracycline Resistance, Thiostrepton, Peptide Elongation Factor G
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