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Identification of the long ubiquitin extension as ribosomal protein S27a

Abstract

Two proteins of unknown function are encoded by 3' in-frame extensions of ubiquitin genes1. The polypeptides are synthesized as an additional 52 (refs 2–4) or 76–80 (refs 4,5) amino acids on the C terminus of ubiquitin, an unusual arrangement conserved in man3,5, yeast4 and plants (J. Callis and R. Vierstra, personal communication). Although not homologous to each other or to ubiquitin, both extension proteins are highly basic and contain patterns of cysteine and histidine similar to those proposed to form 'zinc fingers'6,7. The longer C-terminal extension protein (CEP80) is 30% lysine and arginine and, when denatured, behaves like a small cationic protein8. Its properties after isolation in physiological conditions, however, suggested that CEP80 is part of an RNA-protein complex. Using the antibodies that confirmed the presence of CEP80 in eukaryotic cells8, we show here that the protein is located on ribosomes. Immunoblotting of rat 40S subunit proteins specifically identifies CEP80 as ribosomal protein S27a.

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References

  1. Schlesinger, M. J. & Bond, U. Oxf. Surv. Euk. Genes 4, 77 (1987).

    CAS  Google Scholar 

  2. Müller-Taubenberger, A., Westphal, M., Jaeger, E., Noegel, A. & Gerisch, G. FEBS Lett. 229, 273–278 (1988).

    Article  PubMed  Google Scholar 

  3. Salvensen, G., Lloyd, C. & Farley, D. Nucleic Acids Res. 15, 5485 (1987).

    Article  Google Scholar 

  4. Özkaynak, E., Finley, D., Solomon, M. J. & Varshavsky, A. EMBO J. 6, 1429–1439 (1987).

    Article  PubMed  PubMed Central  Google Scholar 

  5. Lund, P. K. et al. J. biol. Chem. 260, 7609–7613 (1985).

    CAS  PubMed  Google Scholar 

  6. Berg, J. M. Science 232, 485–487 (1986).

    Article  ADS  CAS  PubMed  Google Scholar 

  7. Evans, R. M. & Hollenberg, S. M. Cell 52, 1–3 (1988).

    Article  CAS  PubMed  Google Scholar 

  8. Redman, K. L. & Rechsteiner, M. J. biol. Chem. 263, 4926–4931 (1988).

    CAS  PubMed  Google Scholar 

  9. Collatz, E., Wool, I. G., Lin, A. & Stöffler, G. J. biol. Chem. 251, 4666–4672 (1976).

    CAS  PubMed  Google Scholar 

  10. Collatz, E. et al. J. biol. Chem. 252, 9071–9080 (1977).

    CAS  PubMed  Google Scholar 

  11. Odani, S., Kenmochi, N. & Ogata, K. J. Biochemistry 103, 872–877 (1988).

    Article  CAS  Google Scholar 

  12. Lin, A., Chan, Y.-L., Jones, R. & Wool, I. G. J. biol. Chem. 262, 14343–14351 (1987).

    CAS  PubMed  Google Scholar 

  13. Cornish-Bowden, A. Analyt. Biochem. 105, 233–238 (1980).

    Article  CAS  PubMed  Google Scholar 

  14. McConkey, E. H. et al. Molec. gen. Genet. 169, 1–6 (1979).

    Article  CAS  PubMed  Google Scholar 

  15. Madjar, J.-J., Arpin, M., Buisson, M. & Reboud, J.-P. Molec. gen. Genet. 171, 121–134 (1979).

    Article  CAS  PubMed  Google Scholar 

  16. Hardy, S. J. S. & Kurland, C. G. Biochemistry 5, 3676–3684 (1966).

    Article  CAS  PubMed  Google Scholar 

  17. Nue, H. C. & Heppel, L. A. Proc. natn. Acad. Sci. U.S.A. 51, 1267–1274 (1964).

    Article  ADS  Google Scholar 

  18. Finley, D. et al. in Ubiquitin (ed M. Rechsteiner) 39–75 (Plenum, New York), (1988).

    Book  Google Scholar 

  19. Finley, D., Bartel, B. & Varshavsky, A. Nature (in the press).

  20. Otaka, E., Higo, K. & Osawa, S. Biochemistry 21, 4545–4550 (1982).

    Article  CAS  PubMed  Google Scholar 

  21. Otaka, E. & Osawa, S. Molec. gen. Genet. 181, 176–182 (1981).

    Article  CAS  Google Scholar 

  22. Rechsteiner, M. A. Rev. Cell Biol. 3, 1–30 (1987).

    Article  CAS  Google Scholar 

  23. Nomura, M., Gourse, R. & Baughman, G. A. Rev. Biochem. 53, 75–117 (1984).

    Article  CAS  Google Scholar 

  24. Brown, G. E., Kolb, A. J. & Stanley, W. M. Meth. Enzym 30, 368–387 (1974).

    Article  CAS  PubMed  Google Scholar 

  25. Salinovich, O. & Montelaro, R. C. Analyt. Biochem. 156, 341–347 (1986).

    Article  CAS  PubMed  Google Scholar 

  26. Madjar, J.-J., Michel, S., Cozzone, A. J. & Reboud, J.-P. Analyt. Biochem. 92, 174–182 (1979).

    Article  CAS  PubMed  Google Scholar 

  27. Fling, S. P. & Gregerson, D. S. Analyt. Biochem. 155, 83–88 (1986).

    Article  CAS  PubMed  Google Scholar 

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Redman, K., Rechsteiner, M. Identification of the long ubiquitin extension as ribosomal protein S27a. Nature 338, 438–440 (1989). https://doi.org/10.1038/338438a0

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