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.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Rent or buy this article
Prices vary by article type
from$1.95
to$39.95
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Walter, P. & Blobel, G. Proc. natn. Acad. Sci. U.S.A. 77, 7112–7116 (1980).
Walter, P. & Blobel, G. Nature 99, 691–698 (1982).
Krieg, U. C., Walter, P. & Johnson, A. E. Proc. natn. Acad. Sci. U.S.A. 83, 8604–8608 (1986).
Kurzchalia, T. V. et al. Nature 320, 634–636 (1986).
Gilmore, R., Blobel, G. & Walter, P. J. Cell Biol. 95, 463–469 (1982).
Meyer, D. I., Krause, E. & Dobberstein, B. Nature 297, 647–650 (1982).
Lauffer, L. et al. Nature 318, 334–338 (1985).
Tajima, S., Lauffer, L., Rath, V. L. & Walter, P. J. Cell Biol. 103, 1167–1178 (1986).
Connolly, T. & Gilmore, R. Cell 57, 599–610 (1989).
Saiki, R. K. et al. Science 239, 487–494 (1988).
Byström, A. S., Hjalmarsson, K. J., Wikström, P. M. & Björk, G. R. EMBO J. 2, 899–905 (1983).
Bystrom, A. S. & Björk, G. R. Molec. gen. Genet. 188, 440–446 (1982).
Gill, D. R., Hatfull, G. F. & Salmond, G. P. C. Molec. gen. Genet 205, 134–145 (1986).
Dever, T. E., Glynias, M. J. & Merrick, W. C. Proc. natn. Acad. Sci. U.S.A. 84, 1814–1818 (1987).
Pfeffer, S. & Ullrich, A. Nature 313, 184 (1985).
Williams, A. F. & Barclay, A. N. A. Rev. Immun. 6, 381–405 (1988).
Bourne, H. Cell 53, 669–671 (1988).
Kaziro, Y. Biochim. biophys. Acta 505, 95–127 (1978).
Thompson, R. C. Trends biochem. Sci. 13, 91–93 (1988).
Garnier, J., Osguthorpe, D. J. & Robson, B. J. molec. Biol. 120, 97–120 (1978).
Finer-Moore, J. & Stroud, R. M. Proc. natn. Acad. Sci. U.S.A. 81, 155–159 (1984).
Wiedmann, M., Kurzchalia, T. V., Hartmann, E. & Rapoport, T. A. Nature 328, 830–832 (1987).
von Heijne, G. J. molec. Biol. 184, 99–105 (1985).
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).
Bjorkman, P. J. et al. Nature 329, 512–518 (1987).
Gill, D. R. & Salmond, G. P. C. Molec. gen. Genet. 210, 504–508 (1987).
Koshland, D. & Botstein, D. Cell 30, 893–902 (1982).
Garcia, P. D. & Walter, P. J. Cell Biol. 106, 1043–1048 (1988).
Poritz, M. A., Strub, K. & Walter, P. Cell 55, 4–6 (1988).
Struck, J. C. R., Toschka, H. Y., Specht, T. & Erdmann, V. A. Nucleic. Acids Res. 18, 7740 (1988).
Frohman, M. A., Dush, M. K. & Martin, G. R. Proc. natn. Acad. Sci. U.S.A. 85, 8998–9002 (1988).
Maxam, A. M. & Gilbert, W. Meth. Enzym. 65, 499–560 (1980).
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).
Sanger, F., Nicklen, S. & Coulson, R. Proc. natn. Acad. Sci. U.S.A. 74, 5463–5467 (1977).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
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
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/340482a0
This article is cited by
-
Synergistic action of the gut microbiota in environmental RNA interference in a leaf beetle
Microbiome (2021)
-
Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk
Nature Communications (2019)
-
Genetic Analysis of Protein Translocation
The Protein Journal (2019)
-
The signal recognition particle contacts uL23 and scans substrate translation inside the ribosomal tunnel
Nature Microbiology (2017)
-
Tail-anchor targeting by a Get3 tetramer: the structure of an archaeal homologue
The EMBO Journal (2012)
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.