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Updated: Jul 24, 2026

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation
Published on: February 12, 2022
Distinct modes of signal recognition particle interaction with the ribosome
Martin R Pool1, Joachim Stumm, Tudor A Fulga
1Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), D-69120 Heidelberg, Germany. mrp@zmbh.uni-heidelberg.de
Abstract:
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.
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