A molecular recognition feature mediates ribosome-induced SRP-receptor assembly during protein targeting

Author:

Hwang Fu Yu-Hsien1,Chandrasekar Sowmya1,Lee Jae Ho1,Shan Shu-ou1ORCID

Affiliation:

1. Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA

Abstract

Molecular recognition features (MoRFs) provide interaction motifs in intrinsically disordered protein regions to mediate diverse cellular functions. Here we report that a MoRF element, located in the disordered linker domain of the mammalian signal recognition particle (SRP) receptor and conserved among eukaryotes, plays an essential role in sensing the ribosome during cotranslational protein targeting to the endoplasmic reticulum. Loss of the MoRF in the SRP receptor (SR) largely abolishes the ability of the ribosome to activate SRP-SR assembly and impairs cotranslational protein targeting. These results demonstrate a novel role for MoRF elements and provide a mechanism for the ribosome-induced activation of the mammalian SRP pathway. Kinetic analyses and comparison with the bacterial SRP further suggest that the SR MoRF functionally replaces the essential GNRA tetraloop in the bacterial SRP RNA, providing an example for the replacement of RNA function by proteins during the evolution of ancient ribonucleoprotein particles.

Funder

National Institutes of Health

Gordon and Betty Moore Foundation

Publisher

Rockefeller University Press

Subject

Cell Biology

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