Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20226 (TATA-binding protein)
 1,297 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The mechanisms of transcriptional activation directed by sequence-specific regulators is central to understanding gene regulation. Here, we report the isolation of coactivators responsible for mediating transcriptional activation by Gal4-Pro, a hybrid regulator containing the proline-rich activation domain of human CTF/NFI. Chromatographic studies indicate that endogenous human TFIID consists of a multisubunit complex containing the TATA-binding protein (TBP), coactivators, and other associated factors. A fraction containing the coactivator activity was separated from the endogenous TBP after disrupting the tightly associated complex with urea. The urea-purified TBP was active for basal level transcription but no longer could support activation by Gal4-Pro. However, when the two separated components were added together, activated levels of transcription were restored in the presence of Gal4-Pro. Immunoaffinity purification of the TFIID complex identifies several polypeptides specifically associated with the endogenous TBP, some or all of which function as coactivators when reconstituted with Gal4-Pro. The isolated coactivators also mediate activation by a chimeric glutamine-rich activator derived from Sp1 but not the Gal4-VP16 activator, suggesting distinct factor requirements for different types of transcriptional regulators.
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PMID:Coactivators for a proline-rich activator purified from the multisubunit human TFIID complex. 174 79

Hormone activation of MMTV transcription results in the establishment of a tightly bound transcription factor complex at the promoter (Cordingley et al., Cell 48, 261-270, 1987). We have characterized two fractionable binding activities which participate in this complex. One factor, previously identified as the mouse homologue of NF-1 (or CTF), protects sequences -82 to -56 from exonuclease III digestion in vitro. Sequences protected by a second factor (-42 to -4) span the TATA box of the promoter, suggesting that the binding activity in this fraction is equivalent to the HeLa cell transcription factor TFIID (Sawadogo and Roeder, Cell 43, 165-175, 1986). The downstream boundary of exonuclease protection by the putative TATA-binding factor is -4; DNase1 footprinting of this fraction, however, showed additional protection of discrete sites downstream of the cap site. The apparent concentration and promoter-specific binding activity of both factors is unaffected by hormone treatment of the cells.
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PMID:Binding of multiple factors to the MMTV promoter in crude and fractionated nuclear extracts. 282 33

TFIID is a multisubunit protein complex comprised of the TATA-binding protein (TBP) and multiple TBP-associated factors (TAFs). The TAFs in TFIID are essential for activator-dependent transcription. The cloning of a complementary DNA encoding a human TFIID TAF, TAFII55, that has no known homolog in Drosophila TFIID is now described. TAFII55 is shown to interact with the largest subunit (TAFII230) of human TFIID through its central region and with multiple activators--including Sp1, YY1, USF, CTF, adenoviral E1A, and human immunodeficiency virus-type 1 Tat proteins--through a distinct amino-terminal domain. The TAFII55-interacting region of Sp1 was localized to its DNA-binding domain, which is distinct from the glutamine-rich activation domains previously shown to interact with Drosophila TAFII110. Thus, this human TFIID TAF may be a co-activator that mediates a response to multiple activators through a distinct mechanism.
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PMID:Cloning of an intrinsic human TFIID subunit that interacts with multiple transcriptional activators. 782 54