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General transcription factor TFIID, consisting of TATA-binding protein (TBP) and TBP-associated factors (TAFs), plays a central role in both positive and negative regulation of transcription. The TAF N-terminal domain (TAND) of TAF1 has been shown to interact with TBP and to modulate the interaction of TBP with the TATA box, which is required for transcriptional initiation and activation of TATA-promoter...
Regulation of RNA polymerase II (pol II) transcription is a highly dynamic process requiring the coordinated interaction of an array of regulatory proteins. Central to this process is the TATA-binding protein (TBP), the key component of the multiprotein complex TFIID. Interaction of TBP with core promoters nucleates the assembly of the preinitiation complex and subsequent recruitment of pol II. Despite...
Using the yeast two-hybrid system, we isolated a human cDNA that encodes a protein (hp22) interacting with TATA box-binding factor TFIID subunit p80 containing similarity with histone H4. Sequence analysis showed that the open reading frame (ORF) specifies a 161-amino-acid (aa) polypeptide homologous to Drosophila melanogaster TFIID subunit p22 (dp22). Comparison of the aa sequence of human TFIID...
A cDNA clone encoding a Xenopus laevis (Xl) homologue of human transcription factor IID (TFIID) subunit p80 was isolated and sequenced. The deduced 618-amino-acid (aa) sequence was compared to the homologues from human, mouse, rat and Drosophila melanogaster (Dm). A highly conserved region exists in the central region among these species. In contrast, the C-terminal region has significant homology...
A cDNA encoding a mouse transcription factor IID (TFIID) subunit, containing histone H4 homology, was cloned and sequenced. The predicted 678-amino-acid (aa) sequence of this molecule showed 97 and 41% identity to the human and Drosophila melanogaster homologues, respectively. Four putative direct repeats were found in the most highly conserved region in the central part of this protein.
A cDNA encoding a rat transcription factor IID (TFIID) subunit (p80), with histone H4 homology, was isolated and sequenced. The deduced amino acid (aa) sequence predicts a 678-aa protein with 97% identity to the human and 42% to the Drosophila melanogaster (Dm) homologues. Homologies between three species indicate the presence of three distinct regions.
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