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Published February 18, 2013 | Published
Journal Article Open

SecYEG activates GTPases to drive the completion of cotranslational protein targeting


Signal recognition particle (SRP) and its receptor (SR) comprise a highly conserved cellular machine that cotranslationally targets proteins to a protein-conducting channel, the bacterial SecYEG or eukaryotic Sec61p complex, at the target membrane. Whether SecYEG is a passive recipient of the translating ribosome or actively regulates this targeting machinery remains unclear. Here we show that SecYEG drives conformational changes in the cargo-loaded SRP–SR targeting complex that activate it for GTP hydrolysis and for handover of the translating ribosome. These results provide the first evidence that SecYEG actively drives the efficient delivery and unloading of translating ribosomes at the target membrane.

Additional Information

© 2013 Akopian et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). Submitted: 8 August 2012; accepted: 16 January 2013. We thank Oded Lewinson for help with liposome experiments, Ishu Saraogi for help in cotranslational targeting assays and valuable discussions, and members of the Shan group for comments on the manuscript. This work was supported by National Institutes of Health (NIH) grant GM078024, and career awards from the Henry and Camille Dreyfus foundation and the David and Lucile Packard foundation to S. Shan. D. Akopian was supported by NIH/National Research Service Award training grant 5T32GM07616.

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