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. 2006 Jan 2;172(1):55–66. doi: 10.1083/jcb.200510016

Figure 5.

Figure 5.

Sec4p, Sro7p, and Sec9p form a nucleotide-dependent ternary complex. Glutathione beads with 4 μM of either GTPγS- or GDP-loaded GST-Sec4p (Sec4) or GST alone in the presence of GTPγS were incubated with either purified Sro7p (Sro7) or recombinant Sec9-His6p (Sec9) or both at 1 μM concentrations at 4°C. Copurifying Sro7p or Sec9-His6p were detected by Western blotting using an Sro7p-specific (α-Sro7) or Sec9p-specific (α-Sec9) antibody. The input lanes represent 5% of the total Sro7p or Sec9-His6p. Coomassie staining is shown as a loading control. The asterisk indicates a contaminating protein present on the GST-Sec4 beads that cross reacts with the α-Sec9 antibody.