The acetylation of histone lysine residues plays a crucial role in the epigenetic regulation of gene transcription. A bromodomain is a protein domain that recognizes acetylated lysine residues such as those on the N-terminal tails of histones. This recognition is often a prerequisite for protein-histone association and chromatin remodeling. These domains function in the linking of protein complexes to acetylated nucleosomes, thereby controlling chromatin structure and gene expression. Thus, bromodomains serve as “readers” of histone acetylation marks regulating the transcription of target promoters. TAF1 is a component of transcription factor IID, and binds to core promoter sequences at the transcription start site. TAF1 helps control transcription by both its kinase and histone acetyltransferase enzymatic activities. It interacts with transcriptional activators such as the androgen receptor to promote transcription. Disruption of TAF1 causes dystonia 3 (X-linked torsion dystonia) and decreased apoptosis. This protein product contains the first bromodomain of TAF1.
Physical form
50 mM Tris, pH 7.5, containing 500 mM sodium chloride, 5 mM β-mercaptoethanol and 5% glycerol.
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