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 Jan 15;26(2):185–194. doi: 10.1091/mbc.E14-07-1202

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

© 2015 Mehnert, Sommermeyer, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

“ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.

PMC Copyright notice

FIGURE 2: — Hrd3KR is fully integrated into the HRD-ligase. (A) Microsomes prepared from ∆hrd3 cells expressing plasmid-encoded HA-Hrd3 or HA-Hrd3KR were solubilized with NP40, and the Hrd3 variants were precipitated with anti-HA antibodies under nondenaturing conditions. The bound proteins were analyzed by SDS–PAGE and immunoblotting using the indicated antibodies. (B) HA-tagged Hrd3 variants were precipitated from lysates of yeast cells expressing HA-Hrd3 or HA-Hrd3KR and containing plasmids encoding Hrd3 or Hrd3KR under nondenaturing conditions. The precipitates were analyzed by immunoblotting with the given antibodies. (C) Plasmid-borne Hrd3 or Hrd3KR were expressed in ∆hrd3 Der1-Myc (left) or ∆hrd3 Hrd1-HA (right) cells. Der1-Myc and Hrd1-HA were then purified from solubilized microsomal preparations and the precipitates analyzed by immunoblotting with the indicated antibodies.