Abstract
TFIID is a multisubunit protein containing the TATA box-binding polypeptide (TBP) and associated factors (TFIID-TAFs) required for activated transcription by RNA polymerase II. TBPs from different eukaryotes contain a highly conserved carboxy-terminal domain and very divergent amino-terminal domains. Earlier studies proposed that the amino-terminal domains of metazoan TBPs are required for activated transcription. However, we report that a human TFIID complex containing an amino-terminal truncated TBP contains all the major TFIID-TAFs and supports in vitro transcriptional stimulation by different classes of activation domains and from a TATA-less promoter. Protein blotting experiments revealed direct interactions between the conserved domain of TBP and the two largest TAFs. The results suggest a model for the interaction of TFIID-TAFs with TBP.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 180-187 |
| Number of pages | 8 |
| Journal | Genes and Development |
| Volume | 7 |
| Issue number | 2 |
| DOIs | |
| State | Published - 1993 |
| Externally published | Yes |
Keywords
- RNA polymerase II
- TBP-associated factors
- TFIID
- Transcription factor
- Transcriptional activation
ASJC Scopus subject areas
- General Medicine
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