Upf1 and Dcp2 interact in a manner dependent upon Edc3.

<p>(A) Upf1 was assessed for its ability to interact by yeast two-hybrid analysis with different domains of Dcp2. (B) The Dcp2-Upf1 interaction was further characterized by yeast two-hybrid analysis at the amino acid level. The structure of <i>S. cerevisiae</i> Dcp2 was predicted using the <i>S. pombe</i> Dcp2 crystal structure (PDB:2QKM) <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0026547#pone.0026547-She1" target="_blank">[31]</a>, and point mutations were made along the surface of Dcp2 (102–300) in order to test yeast two-hybrid interaction with Upf1 N-terminus (Nt) and Edc3 full-length (FL). (C) An <i>edc3</i>Δ strain was constructed and interaction between the Upf1 Nt and Dcp2 (102–300), Upf2 C-terminus (Ct), and Pat1 C-terminus (Ct) was assessed by yeast two-hybrid analysis.