TATA-box binding protein (TBP)

TATA-box binding protein (TBP) is a highly conserved general transcription factor essential for the initiation of transcription in eukaryotes[2][3][5]. As the core DNA-binding component of the TFIID complex, TBP recognizes and binds to the TATA-box DNA sequence found approximately 30 bp upstream of many eukaryotic gene promoters, as well as some TATA-less promoters with the help of TBP-associated factors (TAFs)[2][5][7]. Binding of TBP strongly bends the DNA, facilitating assembly of the transcription pre-initiation complex by recruiting additional general transcription factors and RNA polymerase II (and also participates in initiation by RNA polymerases I and III)[2][3][6][7]. Structurally, TBP possesses a saddle-shaped C-terminal domain that interacts with DNA’s minor groove primarily via conserved β-sheet motifs and bulky phenylalanine residues, causing local DNA unwinding necessary for transcriptional machinery access[1][4]. TBP also serves as a hub for protein-protein interactions, forming large complexes with TFIIA, TFIIB, and others[2][4]. The N-terminal region of TBP contains a polyglutamine tract; abnormal expansion of this tract due to CAG repeat mutations leads to spinocerebellar ataxia 17 (SCA17), a neurodegenerative disease[2][3]. TBP’s centrality to gene expression makes it an indispensable factor for cellular function and a focal point in transcriptional regulation research[2][4][7].

Other names

TATA-box-binding proteinTBPGTF2D1TF2DTFIID TBP subunitTBP1TATA sequence-binding proteinTATA-binding factorTATA-box factortranscription initiation factor TFIID TBP subunitSpinocerebellar ataxia 17GTF2DHDL4SCA17TATA-box-binding protein N-terminal domain