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. 2007 May 21;177(4):587–597. doi: 10.1083/jcb.200701043

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Copyright © 2007, The Rockefeller University Press

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Figure 2. — The majority of San does not cofractionate with the NatA complex. (A) San interacts with the NatA complex in a coimmunoprecipitation assay. HA₃-tagged NatH (lanes 1–3), Ard1 (lanes 4–6), and San (lanes 7–9) were individually expressed transiently in 293T cells. The tagged proteins were pulled down with anti-HA beads and the beads were washed in buffers containing 20 mM Tris, pH 8.0, 100–500 mM NaCl, 0.1% NP-40, and 10% glycerol. The proteins on anti-HA beads (P) and 10% of the lysates before (L) and after (S) immunoprecipitation were analyzed by immunoblot assay using antibodies to NatH, Ard1, and San. As a negative control, empty vector was also transfected and analyzed similarly (Mock). α-Tubulin was blotted as the loading control. 293T lysate (S100) was analyzed on a 0–10% sucrose gradient (B), and on a Superdex 200 gel filtration column (C). The standards are indicated below the lanes.