Figure 2.

TAF1 protein domains and functions. DNA and protein interactions are shown. The TAF1 N-terminal (TAND) domain interacts with TBP to inhibit DNA binding [17]. The TAF7-interacting domain binds TAF7 to form a stable complex via a heterodimeric triple barrel (not shown); within this region is a DNA-binding domain, which forms DNA–protein interactions via a winged-helix domain [18]. Towards the C-terminal lies a Zinc knuckle domain (ZnK), which aids in the recruitment of TFIID to endogenous promoters [19]. TAF1 contains tandem bromodomains (BrD1 and BrD2) that bind acetyl-lysines and acyl-lysines, where the second bromodomain of TAF1 binds to butyryl (Bu)- and crotonyl (Cr)-lysine residues on histone tails [20,21]. The diagram shows the relative size of each protein domain, semi-to-scale. Created with BioRender.com.