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A complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteins

Hauser, Stefanie ; Bacher, Gerald ; Dobberstein, Bernhard ; Lütcke, Henrich

In: The EMBO Journal, 14 (1995), Nr. 22. pp. 5485-5493

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Translocation of proteins across the endoplasmic reticulum membrane is initiated by the signal recognition particle (SRP), a cytoplasmic ribonucleoprotein complex consisting of a 7S RNA and six polypeptides. To investigate the functions of the SRP components, we have tested the activities of several SRP subparticles. We show that the SRP GTPase (SRP54) alone binds a signal sequence and discriminates it from a non-signal sequence. Although SRP54 alone is unable to promote translocation, SRP54 in a complex with SRP RNA is both necessary and sufficient to promote translocation of an elongation-arrested nascent protein in a GTPregulated manner. For co-translational translocation, additional SRP components are required. We discuss the implications of our results for the function of the Escherichia coli SRP which is homologous to the SRP54/SRP-RNA complex.

Item Type: Article
Journal or Publication Title: The EMBO Journal
Volume: 14
Number: 22
Date Deposited: 17 Jun 2008 17:33
Date: 1995
Page Range: pp. 5485-5493
Faculties / Institutes: Service facilities > Center for Molecular Biology Heidelberg
Subjects: 570 Life sciences
Uncontrolled Keywords: endoplasmic reticulum , protein translocation , signal recognition particle (SRP) , signal sequence recognition , 4.5S RNA
Schriftenreihe ID: Works by Bernhard Dobberstein
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