Figure 7. Scd6 binds to Dcp2 via multiple elements including the Edc3-binding and leucine-rich motifs and exists in both Edc3- and Pat1-containing decapping complexes.

(A) Two-hybrid analyses of Scd6 interactions with known yeast decapping factors in a WT tester strain. (B) Two-hybrid analyses of Dcp2-bridged interactions between Scd6 and Dcp1 or Edc3. (C) Two-hybrid analyses of interactions between Scd6 and Pat1 or N-terminally truncated Dcp2. (D) Two-hybrid analyses of Scd6 binding to different Dcp2 fragments. See also Figure 7—figure supplement 1. (E) Two-hybrid assays evaluating the consequences of deleting the Dcp2 inhibitory element and the Edc3- or Upf1-binding motifs on Dcp2 interactions with Scd6 and Edc3. (F) Two-hybrid assays evaluating the consequences of deleting the leucine-rich motifs (L₁–L₉) from the Dcp2 C-terminal domain on Dcp2 interactions with Scd6 and Pat1. (G) Two different decapping complexes inferred from two-hybrid analyses in B, E, and F. Allele schematics and two-hybrid analyses as in Figure 1.

Figure 7—figure supplement 1. Scd6 binds to multiple Dcp2 fragments with or without specific overlaps.

A panel of Dcp2 fragments was tested for interaction with Scd6 in two-hybrid assays. The ND244 fragment exhibited strong interaction, the N101-300, N246-330, and ND315 fragments exhibited moderate interaction, and the ND415, F9-C10, F10-C10, F12-C10, and F13-C10 fragments exhibited weak interaction.