Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER
Jae Ho Lee, Ahmad Jomaa, Sangyoon Chung, Yu-Hsien Hwang Fu, Ruilin Qian, Xue-Meng Sun, Hao-Hsuan Hsieh, Sowmya Chandrasekar, Xiaotian Bi, Simone Matteï, Daniel Boehringer, Shimon Weiss, Nenad Ban, Shu‐ou Shan
Abstract
linked to severe congenital neutropenia, uncouples the SRP/SR GTPase cycle from protein translocation. Structures of targeting intermediates reveal the molecular basis of early SRP-SR recognition and emphasize the role of eukaryote-specific elements in regulating targeting. Our results provide a molecular model for the structural and functional transitions of SRP throughout the targeting cycle and show that these transitions provide important points for biological regulation that can be perturbed in genetic diseases.
Topics & Concepts
Chromosomal translocationGTPaseCell biologySignal recognition particleBiophysicsReceptorChemistryBiologySignal peptideGeneBiochemistryPeptide sequenceRNA and protein synthesis mechanismsBacterial Genetics and BiotechnologyRNA Research and Splicing