Sfp1 binds Rpb4 and its efficient import is dependent on RPB4.
(A) RPB4 forms two hybrid interaction with SFP1, but not with FHL1, IFH1 or ABF1. Two-hybrid interaction, using Rpb4 as the bait and the indicated proteins as the preys, was determine by growth on plates lacking leucine, tryptophan, adenine, and histidine supplemented with 5mM of 3-amino-1,2,4-triazole (Uetz et al., 2000). We verified that the growth on the indicator plates was dependent on both plasmids by evicting one plasmid at a time from each of the positive clones (results not shown). (B) GFP-Sfp1 shuttles by a transcription-dependent mechanism. Shuttling of GFP-Sfp1 was determined using nup49-313(ts) mutant cells that are defective in protein import at elevated temperatures (Lee et al., 1996). Wild type (WT, yMS119), nup49-313(ts) (yMS1) and nup49-313 rpb1-1(ts) (yMC4) cells (whose transcription is blocked following a temperature increase to 37°C) expressing GFP-Sfp1 24°C. During mid-log phase, cycloheximide (CHX) (50 μg/ml) was added and the cultures were divided into two samples. One was incubated for at 24°C and the other - at 37°C. To monitor export kinetics, samples were examined microscopically at the indicated time points and photographs of random fields were taken. Cells were classified into those exhibiting nuclear or whole-cell (i.e., cytoplasmic) localization of GFP-Sfp1 (N>200). The proportion of cells exhibiting cytoplasmic localization was plotted as a function of time. Bars represent standard deviation of 3 replicates. (C) Examples of the results at 0 or 3h post re-feeding. Note that, in sated cells, no foci were observed (Fig. S1C).