Structure of a prehandover mammalian ribosomal SRP·SRP receptor targeting complex

Author:

Kobayashi Kan1ORCID,Jomaa Ahmad1ORCID,Lee Jae Ho2,Chandrasekar Sowmya2,Boehringer Daniel1,Shan Shu-ou2,Ban Nenad1ORCID

Affiliation:

1. Department of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Otto-Stern-Weg 5, Zurich CH-8093, Switzerland.

2. Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.

Abstract

First steps of translocation elucidated Ribosomes synthesizing membrane or secretory proteins are targeted to the endoplasmic reticulum (ER) in eukaryotic cells by the signal recognition particle (SRP). Upon reaching the ER, the SRP interacts with its receptor to promote transfer of the signal sequence to the protein-conducting channel or translocon. Kobayashi et al. studied the ribosomal complex that forms on the ER, in which the SRP and its receptor interact to transfer the newly synthesized protein to the translocon. The observed organization of the assembly reveals the roles of multiple eukaryotic-specific protein components present in the SRP and its receptor in stabilizing the conformation that facilitates signal sequence handover. Science , this issue p. 323

Funder

Gordon and Betty Moore Foundation

Swiss National Science Foundation

EMBO

NIH

snsf

SNSF NCCR RNA and disease

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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