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. 2015 Feb 18;11(11):1330–1334. doi: 10.1080/15476286.2014.996457

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© 2014 The Author(s). Published with license by Taylor & Francis Group, LLC

© Klemens Wild and Irmgard Sinning

This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

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Figure 1. — SRP mediated co-translational protein targeting. (A) Scheme of human SRP bound to the ribosome – nascent chain complex (RNC). The S domain recognizes the signal at the ribosomal tunnel exit and the Alu domain binds to the factor binding site (FBS) causing “elongation arrest." (B) RNA gymnastics in SRP S domain assembly. SRP19 (pdb code 3ktv (42) and SRP68-RBD (4p3e (22); and remainder of SRP68/72) are attached in the nucleolus, while the functional particle with SRP54 (1qzw; structure from an archaeal complex⁵⁷) is completed in the cytosol. (C) SRP RNA remodeling of helix 5 and the 5f-loop (orange) by the insertion of an ARM motif (brown) of SRP68-RBD. (D) The assembled SRP S domain bound to the RNC.²⁰ The signal is recognized by SRP54-M (open conformation) and SRP54-NG is flipped to the apex of the particle. The opened SRP RNA 5f-loop is in contact with rRNA.