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Gene Review

ECs4191  -  elongation factor G

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs4191


High impact information on ECs4191

  • Ribosome recycling factor (RRF) disassembles posttermination complexes in conjunction with elongation factor EF-G, liberating ribosomes for further rounds of translation [6].
  • These results show that 4.5S RNA physically associates with the ribosome in performing its essential function, and that this association is mediated by elongation factor G [7].
  • Furthermore, our finding indicates a two-step mechanism of translocation: first, relative rotation of the subunits and opening of the mRNA channel following binding of GTP to EF-G; and second, advance of the mRNA/(tRNA)2 complex in the direction of the rotation of the 30S subunit, following GTP hydrolysis [1].
  • Elongation factor G (EF-G) is a GTPase that is involved in the translocation of bacterial ribosomes along messenger RNA during protein biosynthesis [8].
  • In the canonical scheme, one molecule of GTP is hydrolyzed in the EF-Tu-dependent binding of aa-tRNA to the ribosome, and a second molecule is hydrolyzed in the elongation factor-G (EF-G)-mediated translocation of the polypeptide from the ribosomal A site to the P site [9].

Chemical compound and disease context of ECs4191


Biological context of ECs4191

  • Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome [8].
  • Complementation studies and analyses of the DNA and protein sequences revealed that the tos gene encodes a 59,442-Da protein, with sequence homology to elongation factor EF-G, including G-domain motifs, and that the tos-1 insertion eliminated the C-terminal one-fifth of the protein [15].
  • RF3 is a protein with a molecular weight of 59,460 containing 528 amino acids and displays much similarity to elongation factor EF-G, a GTP binding protein necessary for ribosomal translocation, and other GTP binding proteins known or thought to interact with the ribosome [16].
  • [14C]tRNALys at the P site and Ac[3H]Lys-tRNALys at the A site of poly(A)-primed ribosomes were translocated to the E and P sites, respectively, by means of elongation factor G. The E site-bound [14C]tRNALys could be significantly chased by cognate tRNALys but not by non-cognate tRNAPhe, indicating the coded nature of the E site binding [17].
  • IF-2 levels remain constant as cells double more rapidly, WHEREAS THE EF-G content increases with more rapid cell growth [18].

Anatomical context of ECs4191


Associations of ECs4191 with chemical compounds

  • To restrict the intramolecular mobility, two cysteine residues were engineered into domains 1 and 5 of EF-G that spontaneously formed a disulfide cross-link [23].
  • In contrast, fusidic acid and a GTP analog that fix EF-G to the ribosome, allowing one round of tRNA translocation, inhibited mRNA but not tRNA release from the complex [24].
  • A soluble protein factor was isolated, free of elongation factor (EF)-T and EF-G, based on its ability to stimulate the synthesis of peptide bonds using ribosomal bound 70S-AUG-N-formyl-[35S]methionyl-tRNA complex and added puromycin as substrates [25].
  • Structurally, thiostrepton interferes with EF-G footprints in the alpha-sarcin stem loop (A2660, A2662) located in domain VI of 23S rRNA [26].
  • Function of sulfhydryl groups in ribosome-elongation factor G reactions. Assignment of guanine nucleotide binding site to elongation factor G [27].

Other interactions of ECs4191


Analytical, diagnostic and therapeutic context of ECs4191


  1. A ratchet-like inter-subunit reorganization of the ribosome during translocation. Frank, J., Agrawal, R.K. Nature (2000) [Pubmed]
  2. Elongation factor G participates in ribosome disassembly by interacting with ribosome recycling factor at their tRNA-mimicry domains. Ito, K., Fujiwara, T., Toyoda, T., Nakamura, Y. Mol. Cell (2002) [Pubmed]
  3. Bovine mitochondrial ribosomes. Elongation factor specificity. Eberly, S.L., Locklear, V., Spremulli, L.L. J. Biol. Chem. (1985) [Pubmed]
  4. Phosphorylation of elongation factor G and ribosomal protein S6 in bacteriophage T7-infected Escherichia coli. Robertson, E.S., Aggison, L.A., Nicholson, A.W. Mol. Microbiol. (1994) [Pubmed]
  5. Small clusters of divergent amino acids surrounding the effector domain mediate the varied phenotypes of EF-G and LepA expression. Yaskowiak, E.S., March, P.E. Mol. Microbiol. (1995) [Pubmed]
  6. Orientation of ribosome recycling factor in the ribosome from directed hydroxyl radical probing. Lancaster, L., Kiel, M.C., Kaji, A., Noller, H.F. Cell (2002) [Pubmed]
  7. Mutations in the gene for EF-G reduce the requirement for 4.5S RNA in the growth of E. coli. Brown, S. Cell (1987) [Pubmed]
  8. Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome. Rodnina, M.V., Savelsbergh, A., Katunin, V.I., Wintermeyer, W. Nature (1997) [Pubmed]
  9. Toward a model for the interaction between elongation factor Tu and the ribosome. Weijland, A., Parmeggiani, A. Science (1993) [Pubmed]
  10. Truncated elongation factor G lacking the G domain promotes translocation of the 3' end but not of the anticodon domain of peptidyl-tRNA. Borowski, C., Rodnina, M.V., Wintermeyer, W. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  11. Immunological comparison of the proteins of chicken and rat liver ribosomes. Fischer, N., Stöffler, G., Wool, I.G. J. Biol. Chem. (1978) [Pubmed]
  12. Selective chemical modification of Escherichia coli elongation factor G. N-Ethylmaleimide modification of a cysteine essential for nucleotide binding. Rohrbach, M.S., Bodley, J.W. J. Biol. Chem. (1976) [Pubmed]
  13. Chemical modification in situ of Escherichia coli 50 S ribosomal proteins by the site-specific reagent pyridoxal phosphate. Inactivation of the elongation factor-G-dependent GTPase and of the association with the small ribosomal subunit. Ohsawa, H., Ohsawa, E., Giovane, A., Gualerzi, C. J. Biol. Chem. (1983) [Pubmed]
  14. Purification and characterization of Saccharomyces cerevisiae mitochondrial elongation factor Tu. Rosenthal, L.P., Bodley, J.W. J. Biol. Chem. (1987) [Pubmed]
  15. Identification of the prfC gene, which encodes peptide-chain-release factor 3 of Escherichia coli. Mikuni, O., Ito, K., Moffat, J., Matsumura, K., McCaughan, K., Nobukuni, T., Tate, W., Nakamura, Y. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  16. Localization and characterization of the gene encoding release factor RF3 in Escherichia coli. Grentzmann, G., Brechemier-Baey, D., Heurgue, V., Mora, L., Buckingham, R.H. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  17. Codon-anticodon interaction at the ribosomal E site. Rheinberger, H.J., Sternbach, H., Nierhaus, K.H. J. Biol. Chem. (1986) [Pubmed]
  18. Regulation of initiation and elongation factor levels in Escherichia coli as assessed by a quantitative immunoassay. Krauss, S.W., Leder, P. J. Biol. Chem. (1975) [Pubmed]
  19. Stoichiometry of polypeptide chain elongation. Cabrer, B., San-Millian, M.J., Vazquez, D., Modolell, J. J. Biol. Chem. (1976) [Pubmed]
  20. Purification and characterization of elongation factor G from bovine liver mitochondria. Chung, H.K., Spremulli, L.L. J. Biol. Chem. (1990) [Pubmed]
  21. Purification and properties of rabbit reticulocyte protein synthesis elongation factor 2. Merrick, W.C., Kemper, W.M., Kantor, J.A., Anderson, W.F. J. Biol. Chem. (1975) [Pubmed]
  22. Studies on the inhibition of protein synthesis by selenodiglutathione. Vernie, L.N., Collard, J.G., Eker, A.P., de Wildt, A., Wilders, I.T. Biochem. J. (1979) [Pubmed]
  23. Conformationally restricted elongation factor G retains GTPase activity but is inactive in translocation on the ribosome. Peske, F., Matassova, N.B., Savelsbergh, A., Rodnina, M.V., Wintermeyer, W. Mol. Cell (2000) [Pubmed]
  24. Post-termination complex disassembly by ribosome recycling factor, a functional tRNA mimic. Hirokawa, G., Kiel, M.C., Muto, A., Selmer, M., Raj, V.S., Liljas, A., Igarashi, K., Kaji, H., Kaji, A. EMBO J. (2002) [Pubmed]
  25. Identification of a soluble protein that stimulates peptide bond synthesis. Glick, B.R., Ganoza, M.C. Proc. Natl. Acad. Sci. U.S.A. (1975) [Pubmed]
  26. Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosome. Rodnina, M.V., Savelsbergh, A., Matassova, N.B., Katunin, V.I., Semenkov, Y.P., Wintermeyer, W. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  27. Function of sulfhydryl groups in ribosome-elongation factor G reactions. Assignment of guanine nucleotide binding site to elongation factor G. Marsh, R.C., Chinali, G., Parmeggiani, A. J. Biol. Chem. (1975) [Pubmed]
  28. Characterization of the GTPase reaction of elongation factor Tu. Determination of the stereochemical course in the presence of antibiotic X5108. Eccleston, J.F., Webb, M.R. J. Biol. Chem. (1982) [Pubmed]
  29. Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress. Tamarit, J., Cabiscol, E., Ros, J. J. Biol. Chem. (1998) [Pubmed]
  30. The fourth step of protein synthesis: disassembly of the posttermination complex is catalyzed by elongation factor G and ribosome recycling factor, a near-perfect mimic of tRNA. Kaji, A., Kiel, M.C., Hirokawa, G., Muto, A.R., Inokuchi, Y., Kaji, H. Cold Spring Harb. Symp. Quant. Biol. (2001) [Pubmed]
  31. UGA suppression by a mutant RNA of the large ribosomal subunit. Jemiolo, D.K., Pagel, F.T., Murgola, E.J. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  32. Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome. Cameron, D.M., Thompson, J., March, P.E., Dahlberg, A.E. J. Mol. Biol. (2002) [Pubmed]
  33. Levels of ribosomal protein S1 and elongation factor G in the growth cycle of Escherichia coli. Lambert, J.M., Boileau, G., Howe, J.G., Traut, R.R. J. Bacteriol. (1983) [Pubmed]
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