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Related Experiment Video

Updated: Feb 7, 2026

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

Structure, function and evolution of the signal recognition particle.

Kiyoshi Nagai¹, Chris Oubridge, Andreas Kuglstatter

¹MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK. kn@mrc-lmb.cam.ac.uk

The EMBO Journal

|July 11, 2003

Summary

The signal recognition particle (SRP) is crucial for protein targeting to membranes in prokaryotes and eukaryotes. Recent advancements have significantly improved our understanding of SRP

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Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

The signal recognition particle (SRP) is a vital ribonucleoprotein complex.
It mediates protein targeting to cellular membranes, including the prokaryotic plasma membrane and eukaryotic endoplasmic reticulum.
This process is essential for protein secretion and membrane insertion.

Purpose of the Study:

To summarize recent progress in understanding the architecture and function of the signal recognition particle (SRP).

Main Methods:

The abstract does not specify methods, but implies a review of recent research findings.
Focuses on the mechanism of SRP-mediated protein targeting.

Main Results:

SRP binds to signal peptides on nascent polypeptide chains emerging from ribosomes, forming a ribosome nascent chain (RNC)-SRP complex.
This complex interacts with a membrane-anchored SRP receptor in a GTP-dependent manner.
Proteins are then translocated across or inserted into the membrane via the translocon channel.

Conclusions:

Significant advancements have been made in elucidating the structure and function of SRP.
SRP plays a critical role in the co-translational targeting of proteins to membranes.