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文献和实验octamers can be purified from native sources (Thomas & Butler, 1977) or assembled from recombinant histones (Luger et al, 1999). The latter method allows the incorporation of modified histones, or histone variants. Linker histones H1 and H5 isolated
Purifi cation of Multiprotein Histone Acetyltransferase Complexes
have now been identified and shown to acetylate different sites on histones as well as on non-histone proteins, including transcription regulators. In general, purified recombinant HATs expressed in bacteria or in insect cells are able to acetylate free histones
Histone Deacetylase Activity Assay
that are responsible for the removal of acetyl groups and maintenance of the equilibrium of lysine acetylation on histones. Like most histone modification enzymes, accumulating evidence suggests that many, if not all, HDACs can also modify non-histone proteins
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