Figure 3.
Western-blot analysis indicates mutant ETR1 proteins form disulfide-linked dimers. Membranes isolated from yeast expressing each of the mutant ETR1 proteins were incubated in the presence (+) or absence (−) of 100 mm DTT for 1 h at 37°C, and separated by SDS-PAGE. Western-blot analysis comparing wild-type ETR1 protein to the mutant proteins was carried out using an anti-ETR1 antibody (HRR). In the presence of reducing agent (A), the proteins migrate as a 79-kD monomer, while in the absence of reducing agent (B), a 147-kD dimer is also detected.