Datasets

Title	Ribosome profiling reveals multiple roles of SecA in cotranslational protein export
Organism
Number of Samples	12
Release Date	2021/10/08 00:00
Sequencing Types
Protocol Details

Title
Authors	Zhu Z,Wang S,Shan SO
Journal	Nature communications
Publication Date	2022 Jun 13
Abstract	SecA, an ATPase known to posttranslationally translocate secretory proteins across the bacterial plasma membrane, also binds ribosomes, but the role of SecA's ribosome interaction has been unclear. Here, we used a combination of ribosome profiling methods to investigate the cotranslational actions of SecA. Our data reveal the widespread accumulation of large periplasmic loops of inner membrane proteins in the cytoplasm during their cotranslational translocation, which are specifically recognized and resolved by SecA in coordination with the proton motive force (PMF). Furthermore, SecA associates with 25% of secretory proteins with highly hydrophobic signal sequences at an early stage of translation and mediates their cotranslational transport. In contrast, the chaperone trigger factor (TF) delays SecA engagement on secretory proteins with weakly hydrophobic signal sequences, thus enforcing a posttranslational mode of their translocation. Our results elucidate the principles of SecA-driven cotranslational protein translocation and reveal a hierarchical network of protein export pathways in bacteria. © 2022. The Author(s).
PMC	PMC9192764
PMID	35697696
DOI

Zhu et al. 2022 (PRJNA769692)