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. 1999 Oct;19(10):6621–6631. doi: 10.1128/mcb.19.10.6621

FIG. 6.

FIG. 6

The ADA HAT complex can be rescued by plasmid expression of AHC1. (A and B) Mono Q fractionation of partially purified whole-cell extracts prepared from YJW 103 (ahc1Δ) and YJW 104 (ahc1Δ-pAHC1:HA3). HAT assay fluorograms and Western blots of fractions containing ADA and NuA4 (fractions 14 to 24) are shown. Immunodetection of Ahc1 was accomplished with an anti-HA antibody. The ADA HAT complex was specifically restored in YJW 104 (B) and was absent in the AHC1 deletion (A). HAT assays (C) and Western blots (D) from Superose 6 size exclusion chromatography of Mono Q fractions (A) are shown. Fractions 14 to 20 from a Mono Q column were pooled, concentrated, and fractionated on a Superose 6 column. Ahc1 was immunodetected by monoclonal anti-HA antibody. ADA is present only in YJW 104 bearing pAHC1-HA3 and was eluted at a molecular mass of ∼800 kDa.