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Binding of signal recognition particle gives ribosome/nascent chain complexes a competitive advantage in endoplasmic reticulum membrane interaction

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Item Type:Article
Title:Binding of signal recognition particle gives ribosome/nascent chain complexes a competitive advantage in endoplasmic reticulum membrane interaction
Creators Name:Neuhof, A. and Rolls, M.M. and Jungnickel, B. and Kalies, K.U. and Rapoport, T.A.
Abstract:Most secretory and membrane proteins are sorted by signal sequences to the endoplasmic reticulum (ER) membrane early during their synthesis. Targeting of the ribosome-nascent chain complex (RNC) involves the binding of the signal sequence to the signal recognition particle (SRP), followed by an interaction of ribosome-bound SRP with the SRP receptor. However, ribosomes can also independently bind to the ER translocation channel formed by the Sec61p complex. To explain the specificity of membrane targeting, it has therefore been proposed that nascent polypeptide-associated complex functions as a cytosolic inhibitor of signal sequence- and SRP-independent ribosome binding to the ER membrane. We report here that SRP-independent binding of RNCs to the ER membrane can occur in the presence of all cytosolic factors, including nascent polypeptide-associated complex. Nontranslating ribosomes competitively inhibit SRP-independent membrane binding of RNCs but have no effect when SRP is bound to the RNCs. The protective effect of SRP against ribosome competition depends on a functional signal sequence in the nascent chain and is also observed with reconstituted proteoliposomes containing only the Sec61p complex and the SRP receptor. We conclude that cytosolic factors do not prevent the membrane binding of ribosomes. Instead, specific ribosome targeting to the Sec61p complex is provided by the binding of SRP to RNCs, followed by an interaction with the SRP receptor, which gives RNC-SRP complexes a selective advantage in membrane targeting over nontranslating ribosomes.
Keywords:Competitive Binding, Cytosol, Endoplasmic Reticulum, Intracellular Membranes, Molecular Chaperones, Post-Translational Protein Processing, Protein Binding, Protein Sorting Signals, Proteins, Reticulocytes, Ribosomes, Signal Recognition Particle, Subcellular Fractions, Trans-Activators, Animals, Cattle, Dogs
Source:Molecular Biology of the Cell
ISSN:1059-1524
Publisher:American Society for Cell Biology (U.S.A.)
Volume:9
Number:1
Page Range:103-115
Date:January 1998
Additional Information:Copyright (c) 1998 by The American Society for Cell Biology
Official Publication:http://www.molbiolcell.org/cgi/content/abstract/9/1/103
PubMed:View item in PubMed

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