Intimate functional interactions between TGS1 and the Smn complex revealed by an analysis of the Drosophila eye development
Fig 2
Physical interactions between dTgs1 and the SMN complex.
Proteins co-purifying with dTgs1 or Smn were identified by affinity purification (AP) using GFP-TRAP beads, followed by mass spectrometry (MS) and stringent filtering (see Materials and Methods for details). AP/MS was carried out using 0–3 hr embryos from mothers expressing UAS-GFP-dTgs1 driven by Actin-Gal4 or Smn-GFP under the control of the tubulin promoter. (A) Efficiency of GFP-TRAP-mediated AP assayed using an anti-GFP antibody (T, total protein extract; I, input (10%); S supernatant; IP, immunoprecipitate). (B) Schematic representations of the snRNP maturation pathway; note that in Drosophila there are only four Gemin proteins. See Introduction for a detailed description of this pathway. (C, D) dTgs1 (C) and Smn (D) interacting proteins. All protein IDs conforming to stringent filtering (see Materials and Methods) are shown in the Tables. Mean area corresponds to top 3 protein quantification (T3PQ), the mean of the three highest abundance peptides identified for each protein. The complete lists of the Tgs1- and Smn-interacting proteins are shown in S1 and S2 Tables.