Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2013 Jan-Feb;4(1):18-23.
doi: 10.4161/trns.22601. Epub 2012 Nov 6.

Genomic occupancy of the transcriptional co-activators p300 and CBP

Affiliations
Review

Genomic occupancy of the transcriptional co-activators p300 and CBP

Per-Henrik Holmqvist et al. Transcription. 2013 Jan-Feb.

Abstract

The p300 and CBP co-activators are histone acetylases and central regulators of transcription in metazoans. The genomic occupancy of p300/CBP detected by ChIP-seq experiments can be used to identify transcriptional enhancers. However, studies in Drosophila embryos suggest that there is a preference for some transcription factors in directing p300/CBP to the genome. Although p300/CBP occupancy in general correlates with gene activation, they can also be found at silent genomic regions, which does not result in histone acetylation. Polycomb-mediated H3K27me3 is associated with repression, but does not preclude p300/CBP binding. An antagonism between H3K27ac and H3K27me3 indicates that p300/CBP may be involved in switching between repressed and active chromatin states.

Keywords: CBP; ChIP-seq; Polycomb; enhancer; p300; transcription.

PubMed Disclaimer

Figures

None
Figure 1. (A) Genes that are silenced by Polycomb-mediated H3K27me3 (K27me) can be occupied by p300/CBP. Association of p300/CBP with silent or poised transcriptional enhancers (with or without H3K27me3) does not result in histone acetylation. (B) At active genes, p300/CBP can acetylate histones on H3K27 (K27ac) and H3K18 (not shown), acetylate transcription factors (Ac), function as a scaffolds for recruiting other proteins, or help establish a preinitiation complex by interactions with TFIIB and hypophosphorylated RNA polymerase II.

Similar articles

Cited by

References

    1. Chrivia JC, Kwok RP, Lamb N, Hagiwara M, Montminy MR, Goodman RH. Phosphorylated CREB binds specifically to the nuclear protein CBP. Nature. 1993;365:855–9. doi: 10.1038/365855a0. - DOI - PubMed
    1. Eckner R, Ewen ME, Newsome D, Gerdes M, DeCaprio JA, Lawrence JB, et al. Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor. Genes Dev. 1994;8:869–84. doi: 10.1101/gad.8.8.869. - DOI - PubMed
    1. Whyte P, Williamson NM, Harlow E. Cellular targets for transformation by the adenovirus E1A proteins. Cell. 1989;56:67–75. doi: 10.1016/0092-8674(89)90984-7. - DOI - PubMed
    1. Bedford DC, Kasper LH, Fukuyama T, Brindle PK. Target gene context influences the transcriptional requirement for the KAT3 family of CBP and p300 histone acetyltransferases. Epigenetics. 2010;5:9–15. doi: 10.4161/epi.5.1.10449. - DOI - PMC - PubMed
    1. Wang L, Tang Y, Cole PA, Marmorstein R. Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and function. Curr Opin Struct Biol. 2008;18:741–7. doi: 10.1016/j.sbi.2008.09.004. - DOI - PMC - PubMed

LinkOut - more resources