Highly conserved core domain and unique N terminus with presumptive regulatory motifs in a human TATA factor (TFIID)

Abstract

The factor TFIID is one of several general factors that are necessary and sufficient for transcription initiation by mammalian RNA polymerase II. Stable interactions with the common TATA element lead both to template commitment and to the assembly of the other general factors into a functional preinitiation complex. Consistent with its key role in the promoter activation pathway, human TFIID also seems to be a target for some regulatory factors, as evidenced both by physical and functional studies of interactions between these components. The evolutionary conservation of functional properties led to the purification and cloning of yeast TFIID, the identification of presumptive structural motifs, and direct structure-function studies. Here we report the cloning of a complementary DNA encoding a functional human TFIID. This reveals an evolutionarily conserved core which corresponds precisely to the 180-residue DNA binding/activation domain determined for yeast TFIID, a near absolute conservation of component structural motifs (direct repeats, central basic core/lysine repeat, and sigma homology), providing further support for their functional importance, and a unique N-terminal structure that suggests involvement in species-specific regulatory factor interactions.

Phosphorylation of the N‐terminal domain of Xenopus TATA‐box binding protein by DNA‐dependent protein kinase depends on the C‐terminal core domain

“…2). It has been pointed out that the S-and T-containing motifs in the N-terminal domain of human TBP are reminiscent of the heptapeptide repeats in the CTD of pol II [27]. Like xTBP, the CTD does not have S/T-Q motifs but is nevertheless a good substrate for DNA-PK [23,26].…”

Hepatitis B Virus X Protein Is a Transcriptional Modulator That Communicates with Transcription Factor IIB and the RNA Polymerase II Subunit 5

“…Plasmid pGENK1-CTD was constructed by inserting the annealed complementary oligonucleotides (TCTCCTAGCTACACCCCAACCTCTCCAAGCTACTCA-CCAACA) encoding two repeats of the heptapeptide of the CTD into the EcoRI and BamHI sites of pGENK1. TFIIB and TBP cDNAs were derived from B13 and H10, provided by Dr. M. Hirokoshi (34,35). The inserts were amplified by PCR and inserted into the EcoRI and BamHI sites of pSG5UTPL and pGENK1.…”

Molecular genetic elucidation of the tripartite structure of the Schizosaccharomyces pombe 72 kDa TFIID subunit which contains a WD40 structural motif

“…TFIID is composed of multiple subunits that can be classified into two categories based on their functional roles. One subunit is the TATA box-binding protein, designated TBP, that is essential and sufficient for the basal transcription in vitro (Hoffmann et al 1990). …”