In: The EMBO Journal, 14 (1995), Nr. 22. pp. 5485-5493
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Abstract
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.
Document type: | Article |
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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 |
DDC-classification: | 570 Life sciences |
Uncontrolled Keywords: | endoplasmic reticulum , protein translocation , signal recognition particle (SRP) , signal sequence recognition , 4.5S RNA |
Series: | Works by Bernhard Dobberstein |