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BROMO Domain


No Image A single bromodomain structure is available from HAT coactivator P/CAF (p300/CBP associated factor). The structure is an unusual left-handed up-and-down four helix bundle with a left handed twist. A hydrophobic pocket in the bromodomain creates a binding site for the acetylated moiety. Intermolecular interactions are primarily hydrophobic.

Structure Reference:
Owen, DJ. et al. (2000) EMBO J. 19(22): 6141-9. PDB: 1E6I.

Domain binding and function:
Identified in over one hundred proteins from yeast to man, the approximately 110 amino acid bromodomain can bind to acetylated lysine residues. Acetylation of lysine is a post-translational modification that is particularly notable in the flexible N- and C-terminal tails of histones and, along with methylation of lysines and phosphorylation of serine and threonine residues, is important for coupling histones to changes in chromatin organization and for the epigenetic control of gene expression.  The bromodomain is generally found in proteins that regulate chromatin structure and gene expression such as histone acetyltransferases and the ATPase component of certain nucleosomes-remodeling complexes. The mode of recognition of acetyl-lysine by the Bromo domain is similar to that of acetyl-CoA by histone acetyltransferases, though the bromodomain is the only domain known to interact with acetylated lysine containing peptides.  Recognition of acetyl-lysine by bromodomain proteins is not limited to histones.  This is illustrated by the bromodomain of CREB binding protein transcriptional coactivator (CBP) that recognizes lysine-acetylated p53 at acetyl-lysine 382.   The interaction between the bromodomain and acetyl-p53 is triggered upon DNA damage to promote p53-induced transcriptional activation of the CDK inhibitor p21 and cell cycle arrest.

Examples of Proteins: 
BROMO domain protein
Binding partner Specific Binding motif
CBP (CREB Binding Protein)

Ternary complex factor Elk-1
Not known




Histone H4

Hyperacetylated form of IRF-2

No Image

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