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. 2002 Jul;22(13):4607–4621. doi: 10.1128/MCB.22.13.4607-4621.2002

FIG. 5.

FIG. 5.

DNA binding of Mcm1 alanine mutant proteins in combination with α1. Shown is the affinity of binding to the STE3 α1-Mcm1 site of wild-type (WT) Mcm1 (lanes 3 to 6) and mutant Mcm1 proteins with the V34A (lanes 7 to 10), K40A (lanes 11 to 14), F48A (lanes 15 to 18), Y70A (lanes 19 to 22), S73A (lanes 23 to 26), and S73R (lanes 27 to 30) mutations in the presence of α1. All of the Mcm1 proteins contain the entire MADS box domain (residues 1 to 97) and are titrated as fivefold dilutions from a concentration of 2 × 10−9 M (lanes 3, 7, 11, 15, 19, 23, and 27). Lane 1 contains wild-type Mcm1 in the absence of α1. Lanes 2 to 30 contain 100 ng of partially purified α1. The positions of Mcm1 and the Mcm1-α1 complex are indicated.