An intact conformation at the tip of elongation factor G domain IV is functionally important
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Three variants of Thermus thermophilus EF‐G with mutations in the loop at the distal end of its domain IV were obtained. The replacement of His‐573 by Ala and double mutation H573A/D576A did not influence the functional activity of EF‐G. On the other hand, the insertion of six amino acids into the loop between residues Asp‐576 and Ser‐577 reduced the translocational activity of EF‐G markedly, while its GTPase activity was not affected. It is concluded that the native conformation of the loop is important for the factor‐promoted translocation in the ribosome. The functional importance of the entire EF‐G domain IV is discussed.
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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 [31]
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- Authors
- Martemyanov, K. A., Yarunin, A. S., Liljas, A., & Gudkov, A. T.
- Affiliations
- Russian Academy of Sciences (RU)
- Lund University (SE)
- Corresponding author
- Gudkov, A.T.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1998-08-28
- Volume
- 434
- Issue
- 1-2
- Pages
- 205-208
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1996882817
- Cited by
- 21
- References
- 18
- Citations by year
- 2020: 1 · 2015: 1 · 2012: 1
- FWCI
- 0.81
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Russian Foundation for Basic Research
- 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 Biology › Protein Structure and Dynamics
- Keywords
- elongation factor G, ribosome translocation, Thermus thermophilus, GTPase activity, site-directed mutagenesis, amino acid insertion
- MeSH terms
- Mutation, Peptide Elongation Factors, Protein Conformation, Structure-Activity Relationship, Thermus thermophilus, Peptide Elongation Factor G, GTP Phosphohydrolase-Linked Elongation Factors
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