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  • Title: RNA-mediated interaction between the peptide-binding and GTPase domains of the signal recognition particle.
    Author: Spanggord RJ, Siu F, Ke A, Doudna JA.
    Journal: Nat Struct Mol Biol; 2005 Dec; 12(12):1116-22. PubMed ID: 16299512.
    Abstract:
    The signal recognition particle (SRP) targets nascent proteins to cellular membranes for insertion or secretion by recognizing polypeptides containing an N-terminal signal sequence as they emerge from the ribosome. GTP-dependent binding of SRP to its receptor protein leads to controlled release of the nascent chain into a membrane-spanning translocon pore. Here we show that the association of the SRP with its receptor triggers a marked conformational change in the complex, localizing the SRP RNA and the adjacent signal peptide-binding site at the SRP-receptor heterodimer interface. The orientation of the RNA suggests how peptide binding and GTP hydrolysis can be coupled through direct structural contact during cycles of SRP-directed protein translocation.
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