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Signal recognition particle (SRP), together with its receptor (SR), mediates the targeting of ribosome-nascent chain complexes to the endoplasmic reticulum. Using protein cross-linking, we detected distinct modes in the binding of SRP to the ribosome. During signal peptide recognition, SRP54 is positioned at the exit site close to ribosomal proteins L23a and L35. When SRP54 contacts SR, SRP54 is rearranged such that it is no longer close to L23a. This repositioning may allow the translocon to dock with the ribosome, leading to insertion of the signal peptide into the translocation channel.

Original publication




Journal article



Publication Date





1345 - 1348


Animals, Centrifugation, Density Gradient, Cross-Linking Reagents, Dogs, Guanosine Diphosphate, Guanosine Triphosphate, Guanylyl Imidodiphosphate, Models, Molecular, Plant Proteins, Precipitin Tests, Prolactin, Protein Binding, Protein Precursors, Protein Sorting Signals, Protein Transport, Receptors, Cytoplasmic and Nuclear, Receptors, Peptide, Ribosomal Proteins, Ribosomes, Saccharomyces cerevisiae Proteins, Signal Recognition Particle, Succinimides