Datasets

Title	Targeting and Plasticity of Mitochondrial Proteins Revealed by Proximity-Specific Ribosome Profiling
Organism
Number of Samples	10
Release Date	2014/09/02 00:00
Sequencing Types
Protocol Details

Title
Authors	Jan CH,Williams CC,Weissman JS
Journal	Science (New York, N.Y.)
Publication Date	2014 Nov 7
Abstract	Localized protein synthesis is a fundamental mechanism for creating distinct subcellular environments. Here we developed a generalizable proximity-specific ribosome profiling strategy that enables global analysis of translation in defined subcellular locations. We applied this approach to the endoplasmic reticulum (ER) in yeast and mammals. We observed the large majority of secretory proteins to be cotranslationally translocated, including substrates capable of posttranslational insertion in vitro. Distinct translocon complexes engaged nascent chains at different points during synthesis. Whereas most proteins engaged the ER immediately after or even before signal sequence (SS) emergence, a class of Sec66-dependent proteins entered with a looped SS conformation. Finally, we observed rapid ribosome exchange into the cytosol after translation termination. These data provide insights into how distinct translocation mechanisms act in concert to promote efficient cotranslational recruitment. Copyright © 2014, American Association for the Advancement of Science.
PMC	PMC4285348
PMID	25378630
DOI

Jan et al. 2014 (PRJNA260072)