Domain IV of elongation factor G from Thermus thermophilus is strictly required for translocation
Abstract
Two truncated variants of elongation factor G from Thermus thermophilus with deletion of its domain IV have been constructed and the mutated genes were expressed in Escherichia coli. The truncated factors were produced in a soluble form and retained a high thermostability. It was demonstrated that mutated factors possessed (1) a reduced affinity to the ribosomes with an uncleavable GTP analog and (2) a specific ribosome‐dependent GTPase activity. At the same time, in contrast to the wild‐type elongation factor G, they were incapable to promote translocation. The conclusions are drawn that (1) domain IV is not involved in the GTPase activity of elongation factor G, (2) it contributes to the binding of elongation factor G with the ribosome and (3) is strictly required for translocation. These results suggest that domain IV might be directly involved in translocation and GTPase activity of the factor is not directly coupled with translocation.
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Domain IV in EF-G has been implicated as an important determinant for promoting translocation of the tRNAs.
“This is significant, as domain IV in EF-G has been implicated as an important determinant for promoting translocation of the tRNAs (30, 31, 42).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [30]
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- Authors
- Martemyanov, K. A., & Gudkov, A. T.
- Affiliations
- Russian Academy of Sciences (RU)
- Corresponding author
- Gudkov, Anatoly T
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1999-06-11
- Volume
- 452
- Issue
- 3
- Pages
- 155-159
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2041979337
- Cited by
- 34
- References
- 35
- Citations by year
- 2021: 3 · 2020: 2 · 2016: 3 · 2015: 2 · 2014: 3 · 2013: 1
- FWCI
- 0.57
- 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 › Immunology and Microbiology › Immunology › Toxin Mechanisms and Immunotoxins
- Keywords
- elongation factor G, domain IV, ribosome translocation, GTPase activity, ribosome binding, truncated variants, GTP analogues, Thermus thermophilus, thermal stability, protein structure-function relationship
- MeSH terms
- Cloning, Molecular, Escherichia coli, Guanosine Triphosphate, Guanylyl Imidodiphosphate, Kinetics, Models, Molecular, Peptide Elongation Factors, Recombinant Proteins, Ribosomes, Polymerase Chain Reaction, Mutagenesis, Thermus thermophilus, Sequence Deletion, Protein Structure, Tertiary, Peptide Elongation Factor G, GTP Phosphohydrolase-Linked Elongation Factors
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