TY - JOUR
T1 - Distinct modes of signal recognition particle interaction with the ribosome
AU - Pool, Martin R.
AU - Stumm, Joachim
AU - Fulga, Tudor A.
AU - Sinning, Irmgard
AU - Dobberstein, Bernhard
PY - 2002/8/23
Y1 - 2002/8/23
N2 - 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.
AB - 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.
U2 - 10.1126/science.1072366
DO - 10.1126/science.1072366
M3 - Article
C2 - 12193787
SN - 0036-8075
VL - 297
SP - 1345
EP - 1348
JO - Science
JF - Science
IS - 5585
ER -