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Lee JH, Jomaa A, Chung S, et al. Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER. Sci Adv. 2021;7(21)doi: 10.1126/sciadv.abg0942.
Lee, J. H., Jomaa, A., Chung, S., Hwang Fu, Y. H., Qian, R., Sun, X., Hsieh, H. H., Chandrasekar, S., Bi, X., Mattei, S., Boehringer, D., Weiss, S., Ban, N., & Shan, S. O. (2021). Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER. Science advances, 7(21), . https://doi.org/10.1126/sciadv.abg0942
Lee, Jae Ho, et al. "Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER." Science advances vol. 7,21 (2021). doi: https://doi.org/10.1126/sciadv.abg0942
Lee JH, Jomaa A, Chung S, Hwang Fu YH, Qian R, Sun X, Hsieh HH, Chandrasekar S, Bi X, Mattei S, Boehringer D, Weiss S, Ban N, Shan SO. Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER. Sci Adv. 2021 May 21;7(21). doi: 10.1126/sciadv.abg0942. Print 2021 May. PMID: 34020957; PMCID: PMC8139590.
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Sci Adv. 2021 May 21;7(21). doi: 10.1126/sciadv.abg0942. Print 2021 May.

Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER.

Science advances

Jae Ho Lee, Ahmad Jomaa, SangYoon Chung, Yu-Hsien Hwang Fu, Ruilin Qian, Xuemeng Sun, Hao-Hsuan Hsieh, Sowmya Chandrasekar, Xiaotian Bi, Simone Mattei, Daniel Boehringer, Shimon Weiss, Nenad Ban, Shu-Ou Shan

Affiliations

  1. Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
  2. Department of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland. [email protected] [email protected] [email protected].
  3. Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.
  4. Department of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland.
  5. Cryo-EM Knowledge Hub, ETH Zurich, 8093 Zurich, Switzerland.
  6. Department of Physics, Institute of Nanotechnology and Advanced Materials, Bar-Ilan University, 52900 Ramat-Gan, Israel.
  7. Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA. [email protected] [email protected] [email protected].

PMID: 34020957 PMCID: PMC8139590 DOI: 10.1126/sciadv.abg0942

Abstract

The conserved signal recognition particle (SRP) cotranslationally delivers ~30% of the proteome to the eukaryotic endoplasmic reticulum (ER). The molecular mechanism by which eukaryotic SRP transitions from cargo recognition in the cytosol to protein translocation at the ER is not understood. Here, structural, biochemical, and single-molecule studies show that this transition requires multiple sequential conformational rearrangements in the targeting complex initiated by guanosine triphosphatase (GTPase)-driven compaction of the SRP receptor (SR). Disruption of these rearrangements, particularly in mutant SRP54

Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).

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