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. 2011 Oct 31;6(10):e26547. doi: 10.1371/journal.pone.0026547

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Swisher, Parker.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(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 S. cerevisiae Dcp2 was predicted using the S. pombe Dcp2 crystal structure (PDB:2QKM) [31], 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 edc3Δ 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.