Distinct modes of signal recognition particle interaction with the ribosome
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 …
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 …
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.
AAAS