Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2004 Apr 26;165(2):213–222. doi: 10.1083/jcb.200402100

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2004, The Rockefeller University Press

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 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

PMC Copyright notice

Figure 3. — YidC alone is sufficient to catalyze the membrane insertion of F₀c into proteoliposomes. (A) Co-translational F₀c insertion as well as post-translational proOmpA translocation reactions were performed in the presence of the indicated amounts of (proteo-)liposomes reconstituted with YidC and SecYEG (YidC/SecYEG), YidC alone, SecYEG alone, or without any proteins (−). (B) F₀c insertion efficiency at different (proteo-)liposome concentrations was quantified from the amount of protease-protected material in the presence of SecYEG/YidC (▪), YidC (○), SecYEG (□), or protein-free (•) liposomes. The amount of F₀c synthesized was comparable in all reactions (not depicted) and was set as 100%. All data points shown in B are averages from five independent experiments in which proteoliposomes from three independent reconstitutions were used. Purified SecYEG and YidC were both used at a protein/lipid ratio of 1:100 (wt/wt).