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Evolution of the Translation Termination System in Eukaryotes

  • G. A. Zhouravleva
  • O. V. Tarasov
  • V. V. Schepachev
  • S. E. Moskalenko
  • N. I. Abramson
  • S. G. Inge-Vechtomov

Proteins eRF1 and eRF3 are key components of translation termination in eukaryotes. The highly conserved translation termination factor eRF1 decodes stop codons, while another eukaryotic release factor (RF) eRF3 stimulates eRF1 in GTP-dependent manner. Functional C-terminal domain of eRF3 is necessary for cell viability and reveals high degree of similarity between all known eRF3 and elongation factor eEF1A. Unlike the C-terminal part, the N-terminal region of eRF3 proteins is not conserved and contains ‘prion forming domain’ (PFD). In mammals, eRF3 homologous proteins can be divided into two subfamilies based on the sequence of their N termini, GSPT1 (eRF3a) and GSPT2 (eRF3b). In our work we hypothesize that GSPT2 gene originated through retrotransposition of processed GSPT1 transcript after divergence between placental and marsupial mammals. Data obtained on the order Rodentia indicate that nucleotide sequence encoding N-terminal part of GSPT2 maybe used as a new marker for philogenetic analysis to distinguish between families.

Keywords

Release Factor Translation Termination Cryptic Promoter eRF3 Protein Translation Termination Factor 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Arnason, U., Gullberg, A., Burguete, A.S. and Janke, A. (2000) Molecular estimates of primate divergences and new hypotheses for primate dispersal and the origin of modern humans. Hereditas 133, 217–228.PubMedCrossRefGoogle Scholar
  2. Chauvin, C., Salhi, S., Le Goff, C., Viranaicken, W., Diop, D. and Jean-Jean, O. (2005) Involvement of human release factors eRF3a and eRF3b in translation termination and regulation of the termination complex formation. Mol. Cell Biol. 25, 5801–5811.PubMedCrossRefGoogle Scholar
  3. Doma, M.K. and Parker, R. (2006) Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation. Nature 440, 561–564.Google Scholar
  4. Fandrich, M. and Dobson, C. (2002) The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J. 21, 5682–5690.PubMedCrossRefGoogle Scholar
  5. Faux, N., Bottomley, S., Lesk, A., Irving, J., Morrison, J., de la Banda, M. and Whisstock, J. (2005) Functional insights from the distribution and role of homopeptide repeat-containing proteins. Genome Res. 15, 537–551.PubMedCrossRefGoogle Scholar
  6. Geourjon, C. and Deleage, G. (1994) SOPM: a self-optimized method for protein secondary structure prediction. Protein Eng. 7, 157–164.Google Scholar
  7. Hasegawa, M., Thorne, J.L. and Kishino, H. (2003) Time scale of eutherian evolution estimated without assuming a constant rate of molecular evolution. Genes Genet. Syst. 78, 267–283.PubMedCrossRefGoogle Scholar
  8. Hoshino, S., Imai, M., Mizutani, M., Kikuchi, Y., Hanaoka, F., Ui, M. and Katada, T. (1998) Molecular cloning of a novel member of the eukaryotic polypeptide chain-releasing factors (eRF). Its identification as eRF3 interacting with eRF1. J. Biol. Chem. 273, 22254–22259.PubMedCrossRefGoogle Scholar
  9. Inagaki, Y. and Ford, D.W. (2000) Evolution of the eukaryotic translation terminationsystem: origins of release factors. Mol. Biol. Evol. 17, 882–889.PubMedGoogle Scholar
  10. Inagaki, Y., Blouin, C., Doolittle, W. and Roger, A. (2002) Convergence and constraint in eukaryotic release factor 1 (eRF1) domain 1: the evolution of stop codon specificity. Nucleic Acids Res. 30, 532–544.PubMedCrossRefGoogle Scholar
  11. Inge-Vechtomov, S., Zhouravleva, G. and Philippe, M. (2003) Eukaryotic release factors (eRFs) history. Biol. Cell 95, 195–209.PubMedCrossRefGoogle Scholar
  12. Karlin, S. and Burge, C. (1996) Trinucleotide repeats and long homopeptides in genes and proteins associated with nervous system disease and development. Proc. Natl. Acad. Sci. USA 93, 1560–1565.PubMedCrossRefGoogle Scholar
  13. Kisselev, L., Ehrenberg, M. and Frolova, L. (2003) Termination of translation: interplay of mRNA, rRNAs and release factors? EMBO J. 22, 175–182.PubMedCrossRefGoogle Scholar
  14. Kumar, S., Tamura, K. and Nei, M. (2004) MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief. Bioinf. 5, 150–163CrossRefGoogle Scholar
  15. Le Goff, C., Zemlyanko, O., Moskalenko, S., Berkova, N., Inge-Vechtomov, S., Philippe, M. and Zhouravleva, G. (2002) Mouse GSPT2, but not GSPT1, can substitute for yeast eRF3 in vivo. Genes Cells 7, 1043–1057.PubMedCrossRefGoogle Scholar
  16. Nakamura,Y. and Ito,K. (1998) How protein reads the stop codon and terminates translation. Genes Cells 3, 265–278.PubMedCrossRefGoogle Scholar
  17. Rambaut, A. and Bromham, L. (1998) Estimating divergence dates from molecular sequences. Mol. Biol. Evol. 15, 442–448.PubMedGoogle Scholar
  18. Springer, M.S., Cleven, G.C., Madsen, O., de Jong, W.W., Waddell, V.G., Amrine, H.M. and Stanhope, M.J. (1997) Endemic African mammals shake the phylogenetic tree. Nature 388, 61–64.PubMedCrossRefGoogle Scholar
  19. Urbero, B., Eurwilaichitr, L., Stansfield, I., Tassan J-P., Le Goff, X., Kress, M. and Tuite, M. (1997) Expression of the release factor eRF1 (Sup45p) gene of higher eukaryotes in yeast and mammalian tissues. Biochimie 79, 27–36.PubMedCrossRefGoogle Scholar
  20. Wallrapp, C., Verrier, S., Zhouravleva, G., Philippe, H., Philippe, M., Gress, T. and Jean-Jean, O. (1998) The product of the mammalian orthologue of the Saccharomyces cerevisiae HBS1 gene is phylogenetically related to eukaryotic release factor 3 (eRF3) but does not carry eRF3-like activity. FEBS Lett. 440, 387–392.PubMedCrossRefGoogle Scholar
  21. Zhouravleva, G., Alenin, V., Inge-Vechtomov, S. and Chernoff, Y. (2002) To stick or not to stick: Prion domains from yeast to mammals. Recent Res. Develop. Mol. Cell. Biol. (3), 185–219.Google Scholar
  22. Zhouravleva, G., Schepachev, V., Petrova, A., Tarasov, O. and Inge-Vechtomov, S. (2006) Evolution of translation termination factor eRF3: is GSPT2 generated by retrotransposition of GSPT1's mRNA? IUBMB. Life 58, 199–202.Google Scholar

Copyright information

© Springer Science+Business Media, LLC 2008

Authors and Affiliations

  • G. A. Zhouravleva
    • 1
  • O. V. Tarasov
    • 1
  • V. V. Schepachev
    • 1
  • S. E. Moskalenko
    • 1
  • N. I. Abramson
    • 1
  • S. G. Inge-Vechtomov
    • 1
  1. 1.Department of Genetics and BreedingSt. Petersburg State UniversityRussia

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