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

. 2015 Jul 31;5:12550. doi: 10.1038/srep12550

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

Copyright © 2015, Macmillan Publishers Limited

This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

PMC Copyright notice

(a) Histograms of the maximum height of individual SecA/SecYEG complexes on mica (black dashed; N = 1088; bin size 4 Å) and on glass (red; N = 502; bin size 4 Å) surfaces. The fraction of occurrences in each bin was plotted, the narrowest distribution was taken as the reference and the most highly populated bin was set to 1. The prominent peak at ~4 nm is attributed to the height of the active SecYEG/SecA translocase and agrees well for data acquired on both surfaces. The peak between 1.5 and 3.0 nm corresponds to the height of the cytoplasmic protrusion of SecYEG in the absence of SecA. Periplasmic SecYEG protrusions which are and do not bind SecA were excluded from analysis. (b) Tracking membrane activities for over 30 minutes reveals SecA association, disassociation, and re-association on glass-supported lipid bilayers. At t = 0 s the cytoplasmic SecYEG protrusion is visualized in the membrane. 170s later SecA binds, as indicated by the significant change in protrusion geometry. SecA dissociates at 1190 s. At 1360 s, SecA has re-associated with SecYEG. The scale bar is 10 nm.

Inline graphic — (a) Histograms of the maximum height of individual SecA/SecYEG complexes on mica (black dashed; N = 1088; bin size 4 Å) and on glass (red; N = 502; bin size 4 Å) surfaces. The fraction of occurrences in each bin was plotted, the narrowest distribution was taken as the reference and the most highly populated bin was set to 1. The prominent peak at ~4 nm is attributed to the height of the active SecYEG/SecA translocase and agrees well for data acquired on both surfaces. The peak between 1.5 and 3.0 nm corresponds to the height of the cytoplasmic protrusion of SecYEG in the absence of SecA. Periplasmic SecYEG protrusions which are and do not bind SecA were excluded from analysis. (b) Tracking membrane activities for over 30 minutes reveals SecA association, disassociation, and re-association on glass-supported lipid bilayers. At t = 0 s the cytoplasmic SecYEG protrusion is visualized in the membrane. 170s later SecA binds, as indicated by the significant change in protrusion geometry. SecA dissociates at 1190 s. At 1360 s, SecA has re-associated with SecYEG. The scale bar is 10 nm.