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

. 2013 Oct 1;27(19):2125–2138. doi: 10.1101/gad.226951.113

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

© 2013 Loh et al.; Published by Cold Spring Harbor Laboratory Press

This article, published in Genes & Development, is available under a Creative Commons License (Attribution-NonCommercial 3.0 Unported), as described at http://creativecommons.org/licenses/by-nc/3.0/.

PMC Copyright notice

Figure 5. — SMG7 interacts directly with POP2. (A,B) Interaction of SMG7-V5-SBP-MBP with GFP-POP2 (A) or endogenous POP2/CAF1 (B) in the absence or presence of RNase A. A V5-SBP-MBP served as a negative control. (C) The domain architectures of POP2 and CAF1. POP2 and CAF1 contain a central catalytic domain of the DEDD family exhibiting 84% identity. The C-terminal extensions are more divergent in sequence and length. (D–G) GST-tagged CAF1 or POP2 (wild type or mutants) or GST was used to pull down [³⁵S]-methionine-labeled in vitro translated SMG7 PC and ΔPC fragments. (D,F) Inputs (1%) and bound fractions (16%) were analyzed by 10% SDS-PAGE followed by fluorography. The corresponding Coomassie-stained gels are shown in E and G. (H) GST, GST-POP2, and MBP-SMG7 were expressed in E. coli and purified. The purified proteins were mixed in a 1:1 ratio (inputs), pulled down using glutathione agarose beads, and analyzed by SDS-PAGE followed by Coomassie staining.