InterPro domain: IPR036427

Bromodomains are found in a variety of mammalian, invertebrate and yeast DNA-binding proteins [ 1 ]. Bromodomains are highly conserved alpha-helical motifs that can specifically interact with acetylated lysine residues on histone tails [ 2 , 3 ]. In some proteins, the classical bromodomain has diverged to such an extent that parts of the region are either missing or contain an insertion (e.g., mammalian protein HRX, Caenorhabditis elegans hypothetical protein ZK783.4, yeast protein YTA7). The bromodomain may occur as a single copy, or in duplicate.

This domain is present in proteins involved in a wide range of functions such as acetylating histones, remodeling chromatin, and recruiting other factors necessary for transcription, thus playing a critical role in the regulation of transcription [ 4 ].

The structure of bromodomain is composed of four helices with bundle fold and minor mirror variant of up-and-down topology.

1. The bromodomain: a conserved sequence found in human, Drosophila and yeast proteins. Nucleic Acids Res. 20, 2603
2. The bromodomain revisited. Trends Biochem. Sci. 22, 151-3
3. Bromodomains: Translating the words of lysine acetylation into myelin injury and repair. Neurosci Lett 625, 4-10
4. The role of bromodomain proteins in regulating gene expression. Genes (Basel) 3, 320-43