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Overlapping but Distinct Patterns of Histone Acetylation by the Human Coactivators p300 and PCAF within Nucleosomal Substrates

Open access
Schiltz, R. Louis, Mizzen, Craig A., Vassilev, Alex, Cook, Richard G., Allis, C. David, Nakatani, Yoshihiro·1999·Journal of Biological Chemistry

Abstract

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.

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Metadata

Authors
Schiltz, R. L., Mizzen, C. A., Vassilev, A., Cook, R. G., Allis, C. D., & Nakatani, Y.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1999-01
Volume
274
Issue
3
Pages
1189-1192
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2149666098
Cited by
415
References
6
FWCI
8.48
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Overlapping but Distinct Patterns of Histone Acetylation by the Human Coactivators p300 and PCAF within Nucleosomal Substrates. https://app.cochat.ai/papers/10.1074/jbc.274.3.1189
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Schiltz, R. L., Mizzen, C. A., Vassilev, A., Cook, R. G., Allis, C. D., & Nakatani, Y. (1999). Overlapping but Distinct Patterns of Histone Acetylation by the Human Coactivators p300 and PCAF within Nucleosomal Substrates. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.274.3.1189

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