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Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle

Abstract

PROTEIN targeting to the endoplasmic reticulum in mammalian cells is catalysed by signal recognition particle (SRP)1,2. Cross-linking experiments have shown that the subunit of relative molecular mass 54,000 (Mr 54K; SRP54) interacts directly with signal sequences as they emerge from the ribosome3,4. Here we present the sequence of a complementary DNA clone of SRP54 which predicts a protein that contains a putative GTP-binding domain and an unusually methionine-rich domain. The properties of this latter domain suggest that it contains the signal sequence binding site. A previously uncharacterized Escherichia coli protein has strong homology to both domains. Closely homologous GTP-binding domains are also found in the α-subunit of the SRP receptor (SRα, docking protein) in the endoplasmic reticulum membrane5-8 and in a second E. coli protein, ftsY, which resembles SRα. Recent work has shown that SRα is a GTP-binding protein and that GTP is required for the release of SRP from the signal sequence and the ribosome on targeting to the endoplasmic reticulum membrane9. We propose that SRP54 and SRα use GTP in sequential steps of the targeting reaction and that essential features of such a pathway are conserved from bacteria to mammals.

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References

  1. Walter, P. & Blobel, G. Proc. natn. Acad. Sci. U.S.A. 77, 7112–7116 (1980).

    Article  ADS  CAS  Google Scholar 

  2. Walter, P. & Blobel, G. Nature 99, 691–698 (1982).

    Article  ADS  Google Scholar 

  3. Krieg, U. C., Walter, P. & Johnson, A. E. Proc. natn. Acad. Sci. U.S.A. 83, 8604–8608 (1986).

    Article  ADS  CAS  Google Scholar 

  4. Kurzchalia, T. V. et al. Nature 320, 634–636 (1986).

    Article  ADS  CAS  Google Scholar 

  5. Gilmore, R., Blobel, G. & Walter, P. J. Cell Biol. 95, 463–469 (1982).

    Article  CAS  Google Scholar 

  6. Meyer, D. I., Krause, E. & Dobberstein, B. Nature 297, 647–650 (1982).

    Article  ADS  CAS  Google Scholar 

  7. Lauffer, L. et al. Nature 318, 334–338 (1985).

    Article  ADS  CAS  Google Scholar 

  8. Tajima, S., Lauffer, L., Rath, V. L. & Walter, P. J. Cell Biol. 103, 1167–1178 (1986).

    Article  CAS  Google Scholar 

  9. Connolly, T. & Gilmore, R. Cell 57, 599–610 (1989).

    Article  CAS  Google Scholar 

  10. Saiki, R. K. et al. Science 239, 487–494 (1988).

    Article  ADS  CAS  Google Scholar 

  11. Byström, A. S., Hjalmarsson, K. J., Wikström, P. M. & Björk, G. R. EMBO J. 2, 899–905 (1983).

    Article  Google Scholar 

  12. Bystrom, A. S. & Björk, G. R. Molec. gen. Genet. 188, 440–446 (1982).

    Article  CAS  Google Scholar 

  13. Gill, D. R., Hatfull, G. F. & Salmond, G. P. C. Molec. gen. Genet 205, 134–145 (1986).

    Article  CAS  Google Scholar 

  14. Dever, T. E., Glynias, M. J. & Merrick, W. C. Proc. natn. Acad. Sci. U.S.A. 84, 1814–1818 (1987).

    Article  ADS  CAS  Google Scholar 

  15. Pfeffer, S. & Ullrich, A. Nature 313, 184 (1985).

    Article  ADS  CAS  Google Scholar 

  16. Williams, A. F. & Barclay, A. N. A. Rev. Immun. 6, 381–405 (1988).

    Article  CAS  Google Scholar 

  17. Bourne, H. Cell 53, 669–671 (1988).

    Article  CAS  Google Scholar 

  18. Kaziro, Y. Biochim. biophys. Acta 505, 95–127 (1978).

    Article  CAS  Google Scholar 

  19. Thompson, R. C. Trends biochem. Sci. 13, 91–93 (1988).

    Article  CAS  Google Scholar 

  20. Garnier, J., Osguthorpe, D. J. & Robson, B. J. molec. Biol. 120, 97–120 (1978).

    Article  CAS  Google Scholar 

  21. Finer-Moore, J. & Stroud, R. M. Proc. natn. Acad. Sci. U.S.A. 81, 155–159 (1984).

    Article  ADS  CAS  Google Scholar 

  22. Wiedmann, M., Kurzchalia, T. V., Hartmann, E. & Rapoport, T. A. Nature 328, 830–832 (1987).

    Article  ADS  CAS  Google Scholar 

  23. von Heijne, G. J. molec. Biol. 184, 99–105 (1985).

    Article  CAS  Google Scholar 

  24. Dayhoff, M. O., Eck, R. V. & Park, C. M. in Atlas of Protein Sequence and Structure (ed. Dayhoff, M. O.) 89–99 (National Biomedical Research Foundation, Maryland, 1972).

    Google Scholar 

  25. Bjorkman, P. J. et al. Nature 329, 512–518 (1987).

    Article  ADS  CAS  Google Scholar 

  26. Gill, D. R. & Salmond, G. P. C. Molec. gen. Genet. 210, 504–508 (1987).

    Article  CAS  Google Scholar 

  27. Koshland, D. & Botstein, D. Cell 30, 893–902 (1982).

    Article  CAS  Google Scholar 

  28. Garcia, P. D. & Walter, P. J. Cell Biol. 106, 1043–1048 (1988).

    Article  CAS  Google Scholar 

  29. Poritz, M. A., Strub, K. & Walter, P. Cell 55, 4–6 (1988).

    Article  CAS  Google Scholar 

  30. Struck, J. C. R., Toschka, H. Y., Specht, T. & Erdmann, V. A. Nucleic. Acids Res. 18, 7740 (1988).

    Article  Google Scholar 

  31. Frohman, M. A., Dush, M. K. & Martin, G. R. Proc. natn. Acad. Sci. U.S.A. 85, 8998–9002 (1988).

    Article  ADS  CAS  Google Scholar 

  32. Maxam, A. M. & Gilbert, W. Meth. Enzym. 65, 499–560 (1980).

    Article  CAS  Google Scholar 

  33. Huynh, T. V., Young, R. A. & Davis, R. W. in DNA Cloning, a Practical Approach Vol. 1 (ed. Glover, D. M.) 49–78 (IRL, Oxford, 1985).

    Google Scholar 

  34. Sanger, F., Nicklen, S. & Coulson, R. Proc. natn. Acad. Sci. U.S.A. 74, 5463–5467 (1977).

    Article  ADS  CAS  Google Scholar 

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Bernstein, H., Poritz, M., Strub, K. et al. Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle. Nature 340, 482–486 (1989). https://doi.org/10.1038/340482a0

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