Abstract
Ribosomes translating secretory or membrane proteins are targeted to the protein translocation pore (translocon) in the membrane by the signal recognition particle (SRP) pathway. SRP recognizes hydrophobic signal sequences emerging from the peptide exit region of the ribosome and, with the help of the SRP receptor, mediates the transfer of the translating ribosome to the translocon. The formation of the targeting complex is enhanced by signaling from inside the peptide exit tunnel to the SRP-binding region around the peptide exit, leading to early targeting before the appearance of the nascent peptide outside the ribosome. Furthermore, secondary structure formation of nascent transmembrane segments within the exit tunnel of translocon-bound ribosomes strongly influences the passage of membrane proteins through the translocon. This chapter describes the mechanisms that regulate the early recruitment of SRP to translating ribosomes and the interaction of the latter with the translocon, focusing on the influence of nascent peptide-induced signaling from the exit tunnel to the SRP/translocon-binding site of the ribosome.
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Acknowledgments
We thank Holger Stark for preparing Fig. 5.1.
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Bornemann, T., Holtkamp, W., Wintermeyer, W. (2014). Nascent Peptide-Induced Signaling from the Exit Tunnel to the Outside of the Ribosome. In: Ito, K. (eds) Regulatory Nascent Polypeptides. Springer, Tokyo. https://doi.org/10.1007/978-4-431-55052-5_5
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DOI: https://doi.org/10.1007/978-4-431-55052-5_5
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