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
. 2009 Sep;12(5):659-65.

The role of human bromodomains in chromatin biology and gene transcription

Roberto Sanchez  1 , Ming-Ming Zhou
Affiliations
Review

The role of human bromodomains in chromatin biology and gene transcription

Roberto Sanchez et al. Curr Opin Drug Discov Devel. 2009 Sep.

Abstract

The acetylation of histone lysine is central to providing the dynamic regulation of chromatin-based gene transcription. The bromodomain (BRD), which is the conserved structural module in chromatin-associated proteins and histone acetyltranferases, is the sole protein domain known to recognize acetyl-lysine residues on proteins. Structural analyses of the recognition of lysine-acetylated peptides derived from histones and cellular proteins by BRDs have provided new insights into the differences between and unifying features of the selectivity that BRDs exhibit in binding biological ligands. Recent research has highlighted the importance of BRD/acetyl-lysine binding in orchestrating molecular interactions in chromatin biology and regulating gene transcription. These studies suggest that modulating BRD/acetyl-lysine interactions with small molecules may provide new opportunities for the control of gene expression in human health and disease.

PubMed Disclaimer

Figures

Figure 1
Figure 1. Structural basis of acetyl-lysine recognition by the bromodomain
(A) The 3-D structure of the CREB binding protein (CBP) bromodomain (BRD) bound to a H4K20ac peptide (PDB code: 2RNY); and (B) the acetyl-lysine binding site, showing the key interactions between the CBP BRD and a H4K20ac peptide. The peptide is yellow and the side chains of the protein residues are color-coded by atom type.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Jenuwein T, Allis CD. Translating the histone code. Science. 2001;293(5532):1074–1080. - PubMed
    1. Turner BM. Cellular memory and the histone code. Cell. 2002;111(3):285–291. - PubMed
    1. Nightingale KP, O'Neill LP, Turner B. Histone modifications: Signalling receptors and potential elements of a heritable epigenetic code. Curr Opin Genet Dev. 2006;16(2):125–136. - PubMed
    1. Allfrey VG, Faulkner R, Mirsky AE. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc Natl Acad Sci USA. 1964;51(5):786–794. - PMC - PubMed
    1. Turner BM. Histone acetylation as an epigenetic determinant of long-term transcriptional competence. Cell Mol Life Sci. 1998;54(1):21–31. - PMC - PubMed

Publication types

MeSH terms

LinkOut - more resources