BRD1 Human

Bromodomain Containing 1 (BRD1) is a protein encoded by the BRD1 gene in humans. This protein is part of the bromodomain family, which is known for its role in recognizing acetylated lysine residues on histone tails, thereby playing a crucial role in the regulation of gene expression.

BRD1 contains a bromodomain, an approximately 110 amino acid protein domain that recognizes acetylated lysine residues. This recognition is essential for protein-histone association and chromatin remodeling . The bromodomain adopts an all-α protein fold, forming a hydrophobic pocket that specifically binds to acetylated lysine .

BRD1 is a component of the MOZ/MORF acetyltransferase complex, which stimulates the acetylation of histones H3 and H4. This acetylation is a key step in gene activation, as it loosens the chromatin structure, allowing transcription factors to access DNA . BRD1 plays a significant role in hematopoiesis by directing the specificity of the HBO1 complex towards histone H3 ‘Lys-14’ acetylation, promoting erythroid differentiation .

Variations in the BRD1 gene have been associated with several psychiatric disorders, including schizophrenia and bipolar disorder . The protein’s role in gene activation and chromatin remodeling suggests that it may influence the expression of genes involved in these conditions.

Human recombinant BRD1 is produced in E. coli and is a single, non-glycosylated polypeptide chain containing 156 amino acids. It has a molecular mass of approximately 17.8 kDa and is fused to a 23 amino acid His-tag at the N-terminus for purification purposes .