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. 1999 Sep;19(9):5952–5959. doi: 10.1128/mcb.19.9.5952

FIG. 1.

FIG. 1

Two distinct HAT complexes interact with the GR-τ1 domain. GST pull-down assays were performed with either GST-τ1 or GST alone bound to gluthathione Sepharose beads and the indicated HAT complex. Supernatants (S) and beads (B) were subjected to nucleosomal HAT assays, and reaction mixtures were subjected to SDS-PAGE. Acetylation of histones indicates the presence of SAGA (lanes 1 to 5), NuA4 (lanes 6 to 10 [note that the H3 band is due to contaminating Ada complex]), NuA3 (lanes 11 to 15), or Ada (lanes 16 to 20).

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