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. 2010 Dec 13;286(6):4931–4940. doi: 10.1074/jbc.M110.195024

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FIGURE 3. — Physical interaction between Nej1 and yKu is dependent upon the N-terminal domain of Nej1. A, lane 1, immunoblots of extracts (20 μg) from yeast cells expressing V5-tagged wild-type Nej1 (upper panel), V5-tagged Nej1 lacking the C-terminal domain (middle panel), and V5-tagged Nej1 lacking the N-terminal domain (lower panel). Extracts (200 μg) were incubated with either nickel beads (lane 2) or nickel beads liganded by His-tagged yKu (lane 4). Lane 3, nickel beads liganded by His-tagged Ku incubated with extract expressing the V5 epitope. Epitope-tagged proteins retained by the beads were detected by immunoblotting. B, Coomassie Blue-stained gel showing molecular mass standards (left lane) and purified CBP-Nej1 (300 ng; right lane, pNej1). C, lane 1, immunoblot of purified CBP-Nej1 (100 ng). Purified CBP-Nej1 (1 μg) was incubated with either nickel beads (lane 2) or nickel beads liganded by yKu (lane 3). D, lane 1, immunoblot of purified yKu (100 ng). Purified yKu (1 μg) was incubated without (lane 2) or with (lane 3) purified CBP-Nej1 prior to the addition of protein G-Sepharose beads liganded by anti-CBP antibody. Proteins were detected by immunoblotting with the indicated antibody.