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. 2013 Feb 1;10(2):228–244. doi: 10.4161/rna.23018

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Copyright © 2013 Landes Bioscience

This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.

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graphic file with name rna-10-228-g1.jpg — Figure 1.Dm CCR4 interacts with POP2. (A) Domain organization of Dm CCR4 and POP2. CCR4 contains a LRR domain and a catalytic EEP-nuclease domain (CCR4-C). POP2 consists of a single RNase D-like DEDD family catalytic domain. The numbers beneath the protein outline represent the amino acid position at the fragment/domain boundaries. (B) S2 cells were co-transfected with plasmids expressing GFP-tagged CCR4 (full-length or fragments) and HA-tagged POP2. GFP-tagged firefly luciferase (F-Luc) served as a negative control. Cell lysates were immunoprecipitated with polyclonal anti-GFP antibodies. Inputs (1%) and immunoprecipitates (5% GFP tagged proteins or 30% HA-tagged proteins) were subjected to western blotting using anti-GFP and anti-HA antibodies. (C) Interaction between GFP-tagged POP2 and the indicated CCR4 mutants. (D) Interaction between GFP-tagged CCR4 and the indicated POP2 mutants.