Structure of the Signal Recognition Particle The Signal-Recognition Particle (SRP) is part of a complex of proteins responsible for targeting proteins to specific compartments of the cell. The mechanisms, components and the targeting information appear to be universal, being recognized in plant, animal, and even yeast cells. Proteins destined for targets outside of the cytoplasm (either in membrane-bound compartments, or in the membranes themselves, or for secretion outside the cell), are designated by specific sequences of amino acids in the leader region of the protein. The particle responsible for identifying these specific sequences, called signal peptides in nascent (growing) proteins, is the SRP. This complex consists of a chain of 300 specific bases of RNA and six proteins, identified by their respective molecular weights (in kilodaltons): P9, P14, P54, P68 and P72. It is known that the P54 protein is responsible for reading and interacting with the signal peptide, the two small proteins interact with the ribosome, and the large P68/P72 proteins are involved in the movement of the nascent peptide chain. The SRP will stop protein synthesis after about 70 amino acid residues, in the absence of suitable membrane interactions, preventing the synthesis of proteins in inappropriate environments.