Chimeras of bacterial translation factors Tet(O) and EF‐G
Abstract
Ribosomal protection proteins (RPPs) confer bacterial resistance to tetracycline by releasing this antibiotic from ribosomes stalled in protein synthesis. RPPs share structural similarity to elongation factor G (EF‐G), which promotes ribosomal translocation during normal protein synthesis. We constructed and functionally characterized chimeric proteins of Campylobacter jejuni Tet(O), the best characterized RPP, and Escherichia coli EF‐G. A distinctly conserved loop sequence at the tip of domain 4 is required for both factor‐specific functions. Domains 3–5: (i) are necessary, but not sufficient, for functional specificity; and (ii) modulate GTP hydrolysis by EF‐G, while minimally affecting Tet(O), under substrate turnover conditions.
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Tet(O) shares five structural domains with EF-G; the first two contain the GTP-binding site and are close to the GTP-associated center of the 50S subunit, while the other three are distinct for Tet(O) and associated with its specific functions.
“Sequence homology shows that Tet(O) shares the five structural domains with EF-G, the first two containing the GTP-binding site and being close to the GTP-associated center of the 50S ribosomal subunit, while the other three domains are distinct for Tet(O) and associated with its specific functions 9,10.”
From Mechanism of tetracycline resistance by ribosomal protection protein Tet(O) (2013) · cites this paper as [10]
These results agree with the structural model based on the cryo-EM study, as well as an earlier mutational study of the 507-loop.
“These results agree with the structural model based on our cryo-EM study, as well as an earlier mutational study of the 507-loop 10.”
From Mechanism of tetracycline resistance by ribosomal protection protein Tet(O) (2013) · cites this paper as [10]
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References 27 · Cited by 4
- Authors
- Thakor, N. S., Nechifor, R., Scott, P. G., Keelan, M., Taylor, D. E., & Wilson, K. S.
- Affiliations
- University of Alberta (CA)
- Corresponding author
- Taylor, Diane E.
- Wilson, Kevin S.
- ORCID
- Taylor, Diane E.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2008-03-25
- Volume
- 582
- Issue
- 9
- Pages
- 1386-1390
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2096804416
- Cited by
- 4
- References
- 27
- Citations by year
- 2015: 1 · 2013: 1
- FWCI
- 0.27
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- 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
- ribosomal protection proteins, tetracycline resistance, elongation factor G, tetO, fusion protein, Campylobacter jejuni, Escherichia coli, ribosome translocation, GTP hydrolysis, protein synthesis
- MeSH terms
- Bacterial Proteins, Carrier Proteins, Electrophoresis, Polyacrylamide Gel, Models, Molecular, Protein Conformation, Recombinant Fusion Proteins, Protein Biosynthesis, Blotting, Western, Peptide Elongation Factor G
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