Cited by 21RNA and protein synthesis mechanismsBacterial Genetics and BiotechnologyProtein Structure and Dynamics

An intact conformation at the tip of elongation factor G domain IV is functionally important

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Martemyanov, K.A., Yarunin, A.S., Liljas, A., Gudkov, A.T.·1998·FEBS Letters

Abstract

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).”

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Research works printed but not linked: 3

  1. Martemyanov, K.A., Liljas, A. and Gudkov, A.T. (1998) Bio- chemistry (Moscow) 63 (in press).
  2. Kohno, K., Uchida, T., Ohkuro, H., Nakanishi, S., Nakanishi, T., Fukui, T., Ohtsuka, E., Ikehara, M. and Okada, Y. (1986) Proc. Natl. Acad. Sci. USA 83, 4978^4982.
  3. Ito, K., Ebihara, K., Uno, M. and Nakamura, Y. (1996) Proc. Natl. Acad. Sci. USA 93, 5443^5448.

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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
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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