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J Biol Chem, Vol. 274, Issue 3, 1189-1192, January 15, 1999
,
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From the A number of transcriptional coactivators possess
intrinsic histone acetylase activity, providing a direct link between
hyperacetylated chromatin and transcriptional activation. We have
determined the core histone residues acetylated in vitro by
recombinant p300 and PCAF within mononucleosomes. p300 specifically
acetylates all sites of histones H2A and H2B known to be acetylated in
bulk chromatin in vivo but preferentially acetylates
lysines 14 and 18 of histone H3 and lysines 5 and 8 of histone H4. PCAF
primarily acetylates lysine 14 of H3 but also less efficiently
acetylates lysine 8 of H4. PCAF in its native form, which is present in
a stable multimeric protein complex lacking p300/CBP, primarily acetylates H3 to a monoacetylated form, suggesting that PCAF-associated polypeptides do not alter the substrate specificity. These distinct patterns of acetylation by the p300 and PCAF may contribute to their
differential roles in transcriptional regulation.
Laboratory of Molecular Growth Regulation,
National Institute of Child Health and Human Development, National
Institutes of Health, Bethesda, Maryland 20892, the ¶ Department
of Biology, University of Rochester, Rochester, New York 14627, and the ** Department of Microbiology and Immunology, Baylor
College of Medicine, Houston, Texas 77030
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