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. 2005 Dec;25(23):10419–10432. doi: 10.1128/MCB.25.23.10419-10432.2005

FIG. 10.

FIG. 10.

Ytm1 and Nop7 directly interact with Erb1. (A) Synthetic radiolabeled proteins (*) were incubated with GST fusion proteins (lanes 2, 5, and 8). As negative controls, synthetic peptides were incubated with GST beads only (lanes 1, 4, and 7) or GST fusion proteins were incubated with the unrelated, radiolabeled 40S ribosome assembly factor Krr1 or ribosomal protein L11 (lanes 3, 6, and 9). (B) Radiolabeled wild-type Ytm1 protein was preincubated at 37°C for 15 min (lane 2). Mutant Ytm1-1 protein was preincubated at 37°C for 15 min (lane 3), 30 min (lane 4), or 60 min (lane 5). Following preincubation, wild-type Ytm1 or mutant Ytm1-1 radiolabeled protein was incubated with GST-Erb1. Mutant Ytm1-1 protein was incubated with GST beads only (lane 1) as a negative control. Complexes were eluted from glutathione beads, subjected to electrophoresis on 10% polyacrylamide gels, and detected by autoradiography. (C) Model for interactions between Ytm1, Erb1, and Nop7. Gray lines indicate interactions detected using GST pulldown assays, whereas the black line indicates interactions detected by two-hybrid assays.