| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 25171 | Journal of Biotechnology | 2007 | 8 Pages |
Abstract
We describe a simple, robust, and relatively inexpensive non-radioactive in vitro assay for measuring histone acetyl-transferase activity. The assay takes advantage of easy to purify recombinant E. coli-derived fusion proteins containing the NH2-terminal tails of histones H3 and H4 linked to epitope-tagged maltose-binding protein (MBP), and immunoblotting with antibodies specific to acetylated H3 and H4. Here we show the specificity and dynamic range of this assay for the histone acetyl-transferases, p300 and PCAF. This assay may be adapted readily for other substrates by simply generating new fusion proteins and for other acetyl-transferases by modifying reaction conditions.
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Authors
David Kuninger, James Lundblad, Anthony Semirale, Peter Rotwein,