Signal-sequence recognition by an Escherichia coli ribonucleoprotein complex (original) (raw)

Nature volume 359, pages 741–743 (1992)Cite this article

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 (_M_r 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 coli_5–7 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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Author notes

  1. Joen Luirink
    Present address: Department of Molecular Microbiology, Faculty of Biology, De Boelelaan 1087, 1081 HV, Amsterdam, The Netherlands

Authors and Affiliations

  1. European Molecular Biology Laboratory, Postfach 102209, Meyerhofstrasse 1, 6900, Heidelberg, Germany
    Joen Luirink, Stephen High, Heather Wood, Angelika Giner, David Tollervey & Bernhard Dobberstein

Authors

  1. Joen Luirink
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  2. Stephen High
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  3. Heather Wood
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  4. Angelika Giner
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  5. David Tollervey
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  6. Bernhard Dobberstein
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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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