Letter | Published:

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

Naturevolume 372pages701703 (1994) | Download Citation

Subjects

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.

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.

from$8.99

All prices are NET prices.

References

  1. 1

    Craigen, W. J., Lee, C. C. & Caskey, C. T. Molec. Microbiol. 4, 861–865 (1990).

  2. 2

    Grentzmann, G., Brechemier-Baey, D., Heurgue, V., Mora, L. & Buckingham, R. H. Proc. natn. Acad. Sci. U.S.A. 91, 5848–5852 (1994).

  3. 3

    Mukini, O. et al. Proc. natn. Acad. Sci. U.S.A. 91, 5798–5802 (1994).

  4. 4

    Pel, H. J., Maat, C., Rep, M. & Grivell, L. A. Nucleic Acids Res. 20, 6339–6346 (1992).

  5. 5

    Beaudet, A. L. & Caskey, C. T. Proc. natn. Acad. Sci. U.S.A. 68, 619–624 (1971).

  6. 6

    Grenett, H. E., Bounelis, P. & Fuller, G. M. Gene 110, 239–243 (1992).

  7. 7

    Tassan, J. P. et al. Molec. cell. Biol. 13, 2815–2821 (1993).

  8. 8

    Inge-Vechtomov, S. G. & Andrianova, V. M. Genetika 6, 103–115 (1970).

  9. 9

    Surguchov, A. P., Smirnov, V. N., Ter-Avanesyan, M. D. & Inge-Vechtomov, S. G. Physico-chemical Biology Reviews Vol. 4 (ed. Skulachev, V. P.) 147–205 (Harwood, Reading, 1984).

  10. 10

    Breining, P. & Piepersberg, W. Nucleic Acids Res. 14, 5187–5197 (1986).

  11. 11

    Himmelfarb, H. J., Maicas, E. & Friesen, J. D. Molec. cell. Biol. 5, 816–822 (1985).

  12. 12

    Stansfield, I., Grant, C. M., Akhmaloka & Tuite, M. F. Molec. Microbiol. 6, 3469–3478 (1992).

  13. 13

    Goldstein, J. L., Beaudet, A. L. & Caskey, C. T. Proc. natn. Acad. Sci. U.S.A. 67, 99–106 (1970).

  14. 14

    Konecki, D. S., Aune, K. S., Tate, W. P. & Caskey, C. T. J. biol. Chem. 252, 4514–4520 (1977).

  15. 15

    Caskey, C. T., Beaudet, A. L. & Tate, W. P. Meth. Enzym. 30, 293–303 (1974).

  16. 16

    Lee, C. C., Craigen, W. J., Muzny, D. M., Harlow, E. & Caskey, C. T. Proc. natn. Acad. Sci. U.S.A. 87, 3508–3512 (1990).

  17. 17

    Garret, M. et al. Biochemistry 30, 7809–7817 (1991).

  18. 18

    Frolova, L. Yu., Sudomoina, M. A., Grigorieva, A. Yu., Zinovieva, O. L. & Kisselev, L. L. Gene 109, 291–296 (1991).

  19. 19

    Frolova, L. Yu. et al. EMBO J. 12, 4013–4019 (1993).

  20. 20

    Rasmussen, H. H. et al. Electrophoresis 12, 873–882 (1991).

  21. 21

    Tuite, M. F., Stansfield, I., Eurwilaichitr, L. & Akhmaloka Biochem. Soc. Trans. 21, 857–862 (1993).

  22. 22

    Pel, N. J., Rep, M. & Grivell, L. A. Nucleic Acids Res. 20, 4423–4428 (1992).

  23. 23

    Tate, W. P. & Caskey, C. T. in Ribosomes and Protein Synthesis. A Practical Approach (ed. Spedding, G.) 81–100 (IRL, Oxford. 1990).

  24. 24

    Sawin, K. E., Le Guellec, K., Philippe, M. & Mitchison, T. J. Nature 359, 540–543 (1992).

  25. 25

    Beggs, J. D. Nature 275, 104–109 (1978).

Download references

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

Authors

  1. Search for Lyudmila Frolova in:

  2. Search for Xavier Le Goff in:

  3. Search for Hanne H. Rasmussen in:

  4. Search for Sergey Cheperegin in:

  5. Search for Gabriele Drugeon in:

  6. Search for Michel Kress in:

  7. Search for Inga Arman in:

  8. Search for Anne-Lise Haenni in:

  9. Search for Jullo E. Celis in:

  10. Search for Michel Phllippe in:

  11. Search for Just Justesen in:

  12. Search for Lev Kisselev in:

About this article

Publication history

Received

Accepted

Issue Date

DOI

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

Further reading

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.