Letter | Published:

A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor

Nature volume 372, pages 701703 (15 December 1994) | Download Citation

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Abstract

THE termination of protein synthesis in ribosomes is governed by termination (stop) codons in messenger RNAs and by polypeptide chain release factors (RFs). Although the primary structure of prokaryotic RFs and yeast mitochrondrial RF is established1–4, that of the only known eukaryotic RF (eRF)5 remains obscure. Here we report the assignment of a family of tightly related proteins (designated eRFl) from lower and higher eukaryotes which are structurally and functionally similar to rabbit eRF. Two of these proteins, one from human6 and the other from Xenopus laevis7 , have been expressed in yeast and Escherichia coli, respectively, purified and shown to be active in the in vitro RF assay. The other protein of this family, sup45 (supl) of Saccharomyces cerevisiae, is involved in omnipotent suppression during translation8–12. The amino-acid sequence of the eRFl family is highly conserved. We conclude that the eRFl proteins are directly implicated in the termination of translation in eukaryotes.

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Author information

Affiliations

  1. Department of Molecular Biology, University of Aarhus, DK-800 Aarhus C, Denmark

    • Lyudmila Frolova
    •  & Just Justesen
  2. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 117984 Moscow, Russia

    • Lyudmila Frolova
    •  & Lev Kisselev
  3. Institut Jacques Monod, 75251 Paris Cedex 05, France

    • Lyudmila Frolova
    • , Gabriele Drugeon
    •  & Anne-Lise Haenni
  4. Département de Biologie et Génétique du Développement, CNRS URA 256, Université de Rennes I, 35042 Rennes Cedex, France

    • Xavier Le Goff
    •  & Michel Phllippe
  5. Institute of Medical Biochemistry and Danish Center for Human Genome Research, University of Aarhus, DK-8000 Aarhus C, Denmark

    • Hanne H. Rasmussen
    •  & Jullo E. Celis
  6. Institute of Molecular Genetics, Russian Academy of Sciences, 123182 Moscow, Russia

    • Sergey Cheperegin
    •  & Inga Arman
  7. Laboratoire d'Oncologie Moléculaire, CNRS ERS0048, 94802 Villejuif Cedex, France

    • Michel Kress

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https://doi.org/10.1038/372701a0

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