Literature DB >> 17698235

A non-isotopic in vitro assay for histone acetylation.

David Kuninger1, James Lundblad, Anthony Semirale, Peter Rotwein.   

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 NH(2)-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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Year:  2007        PMID： 17698235      PMCID： PMC2099255          DOI： 10.1016/j.jbiotec.2007.07.498

Source DB:  PubMed          Journal:  J Biotechnol        ISSN： 0168-1656            Impact factor:   3.307


  22 in total

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  8 in total

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