Other: BROMO Domain
The Bromodomain of Gcn5p binding acetylated lysine (red).
Domain Binding and Function
Approximately 110 amino acids in length, the Bromo domain is found in many chromatin-associated proteins such as histone acetylases and the ATPase component of certain nucleosome-remodeling complexes. Bromo domains have been identified in over 100 proteins from yeast to man. The Bromo domains of PCAF and Gcn5p have been shown to interact specifically with peptides containing acetylated lysine residues. Recognition of acetyl-lysine 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.
Structure Reference
- Owen, D.J. et al. (2000) EMBO J. 19(22), 6141–6149.
Examples of Domain Proteins
Binding Examples
| BROMO Domain Proteins | Binding Partners | Domain Binding Sites |
|---|---|---|
| PCAF | Tat | BSYGRKAcKRRQRC |
| CRBP (CREB Binding Protein) | Ternary complex factor Elk-1 | Not known |
| Gcn5p | Histone H4 | AKAcRHR |
| Celtix-1 | IRF-2 | Hyperacetylated form of IRF-2 |
