Abstract
HYDROPHOBIC signal-sequences direct the transfer of secretory proteins across the inner membrane of prokaryotes and the endoplasmic reticulum membranes of eukaryotes1. In mammalian cells, signal-sequences are recognized by the 54K protein (Mr 54,000) of the signal recognition particle (SRP)2,3 which is believed to hold the nascent chain in a translocation-competent conformation until it contacts the endoplasmic reticulum membrane4. The SRP consists of a 7S RNA and six different polypeptides. The 7S RNA and the 54K signal-sequence-binding protein (SRP54) of mammalian SRP exhibit strong sequence similarity to the 4.5S RNA and P48 protein (Ff h) of Escherichia coli5–7 which form a ribonucleoprotein particle. Depletion of 4.5S RNA or overproduction of P48 causes the accumulation of the β-lactamase precursor, although not of other secretory proteins8,9. Whether 4.5S RNA and P48 are part of an SRP-like complex with a role in protein export is controversial. Here we show that the P48/4.5S RNA ribonucleoprotein complex interacts specifically with the signal sequence of a nascent secretory protein and therefore is a signal recognition particle.
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References
von Heijne, G. Biochim. biophys. Acta 947, 307–333 (1988).
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).
Rapoport, T. A. Trends biochem. Sci. 15, 355–358 (1990).
Poritz, M. A., Strub, K. & Walter, P. Cell 55, 4–6 (1988).
Römisch, K. et al. Nature 340, 478–482 (1989).
Bernstein, H. D. et al. Nature 340, 482–486 (1989).
Poritz, M. A. et al. Science 250, 1111–1117 (1990).
Ribes, V., Römisch, K., Giner, A., Dobberstein, B. & Tollervey, D. Cell 63, 591–600 (1990).
Brown, S. New Biol. 3, 430–438 (1991).
Wiedmann, M., Kurzchalia, T. V., Bielka, H. & Rapoport, T. A. J. Cell Biol. 104, 201–208 (1987).
High, S., Görlich, D., Wiedmann, M., Rapoport, T. A. & Dobberstein, B. J. Cell Biol. 113, 35–44 (1991).
Brown, S. & Fournier, M. J. J. Cell Biol. 178, 533–550 (1984).
Randall, L. L. & Hardy, S. J. S. Science 243, 1156–1159 (1989).
Kumamoto, C. A. Molec. Microbiol. 5, 19–22 (1991).
Langer, T. et al. Nature 356, 683–689 (1992).
High, S., Flint, N. & Dobberstein, B. J. Cell Biol. 113, 25–34 (1991).
Römisch, K., Webb, J., Lingelbach, K., Gausepohl, H. & Dobberstein, B. J. Cell Biol. 111, 1793–1802 (1990).
Walter, P. & Blobel, G. Meth. Enzym. 96, 682–691 (1983).
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Luirink, J., High, S., Wood, H. et al. Signal-sequence recognition by an Escherichia coli ribonucleoprotein complex. Nature 359, 741–743 (1992). https://doi.org/10.1038/359741a0
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DOI: https://doi.org/10.1038/359741a0
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