Sk. Burley et Rg. Roeder, BIOCHEMISTRY AND STRUCTURAL BIOLOGY OF TRANSCRIPTION FACTOR-IID (TFIID), Annual review of biochemistry, 65, 1996, pp. 769-799
Eukaryotes have three distinct RNA polymerases that catalyze transcrip
tion of nuclear genes. RNA polymerase II is responsible for transcribi
ng nuclear genes encoding the messenger RNAs and several small nuclear
RNAs. Like RNA polymerases I and III, pol II cannot recognize its tar
get promoter directly and initiate transcription without accessory fac
tors. Instead, this large multisubunit enzyme relies on both general t
ranscription factors and transcriptional activators and coactivators t
o regulate transcription from class II promoters. At the center of thi
s process is TFIID, a 700-kD complex composed of the TATA box binding
protein (TBP) and a set of phylogenetically conserved, polymerase-spec
ific TBP-associated factors or TAF(II)s. Together, TBP and the TAF(II)
s direct assembly of the transcription machinery and play critical reg
ulatory roles in eukaryotic gene expression.