Initiation Factor IF2, Thiostrepton and Micrococcin Prevent the Binding of Elongation Factor G to the Escherichia coli Ribosome
Abstract
The bacterial translational GTPases (initiation factor IF2, elongation factors EF-G and EF-Tu and release factor RF3) are involved in all stages of translation, and evidence indicates that they bind to overlapping sites on the ribosome, whereupon GTP hydrolysis is triggered. We provide evidence for a common ribosomal binding site for EF-G and IF2. IF2 prevents the binding of EF-G to the ribosome, as shown by Western blot analysis and fusidic acid-stabilized EF-G.GDP.ribosome complex formation. Additionally, IF2 inhibits EF-G-dependent GTP hydrolysis on 70 S ribosomes. The antibiotics thiostrepton and micrococcin, which bind to part of the EF-G binding site and interfere with the function of the factor, also affect the function of IF2. While thiostrepton is a strong inhibitor of EF-G-dependent GTP hydrolysis, GTP hydrolysis by IF2 is stimulated by the drug. Micrococcin stimulates GTP hydrolysis by both factors. We show directly that these drugs act by destabilizing the interaction of EF-G with the ribosome, and provide evidence that they have similar effects on IF2.
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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 [7]
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- Authors
- Cameron, D. M., Thompson, J., March, P. E., & Dahlberg, A. E.
- Affiliations
- Brown University (US)
- UNSW Sydney (AU)
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2002-05
- Volume
- 319
- Issue
- 1
- Pages
- 27-35
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2043990613
- Cited by
- 99
- References
- 40
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 1 · 2022: 2 · 2021: 3 · 2020: 2 · 2019: 5 · 2018: 3 · 2017: 1 · 2016: 2 · 2015: 2 · 2013: 6 · 2012: 2
- FWCI
- 4.06
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Australian Research Council
- National Institute of General Medical Sciences (GM19756)
- 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 › Immunology and Microbiology › Immunology › Toxin Mechanisms and Immunotoxins
- Keywords
- elongation factor G, thiostrepton, ribosome binding site, GTP hydrolysis, fusidic acid, antibiotic mechanism of action, Escherichia coli ribosome, elongation factor Tu
- MeSH terms
- Anti-Bacterial Agents, Bacteriocins, Binding, Competitive, Escherichia coli, Guanosine Triphosphate, Hydrolysis, Mutation, Peptide Initiation Factors, Peptides, Protein Binding, Ribosomal Proteins, Ribosomes, RNA, Ribosomal, 23S, Thiostrepton, Time Factors, Blotting, Western, Peptide Elongation Factor G, Escherichia coli Proteins, Prokaryotic Initiation Factor-2
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