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

Using coexpression in COS cells, we have identified novel interactions between the human TATA-binding protein-associated factor 28 (hTAF(II)28) component of transcription factor IID and the ligand binding domains (LBDs) of the nuclear receptors for vitamin D3 (VDR) and thyroid hormone (TRalpha). Interaction between hTAF(II)28 and the VDR and TR LBDs was ligand-reversible, whereas no interactions between hTAF(II)28 and the retinoid X receptors (RXRs) or other receptors were observed. TAF(II)28 interacted with two regions of the VDR, a 40-amino acid region spanning alpha-helices H3-H5 and alpha-helix H8. Interactions were also observed with the H3-H5 region of the TRalpha but not with the equivalent highly related region of the RXRgamma. Fine mapping using RXR derivatives in which single amino acids of the RXRgamma LBD have been replaced with their VDR counterparts shows that the determinants for interaction with hTAF(II)28 are located in alpha-helix H3 and are not identical to those previously identified for interactions with hTAF(II)55. We also describe a mutation in the H3-H5 region of the VDR LBD, which abolishes transactivation, and we show that interaction of hTAF(II)28 with this mutant is no longer ligand-reversible.
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PMID:The human transcription factor IID subunit human TATA-binding protein-associated factor 28 interacts in a ligand-reversible manner with the vitamin D(3) and thyroid hormone receptors. 1074 85

Type I interferon (IFN) stimulates transcription through a heteromeric transcription factor that contains tyrosine-phosphorylated STAT2. We show that STAT2 recruits histone acetyltransferases (HAT) through its transactivation domain, resulting in localized transient acetylation of histones. GCN5, but not p300/CBP or PCAF, is required for STAT2 function. However, GCN5 function is impaired by the transcriptional antagonist, adenovirus E1A oncoprotein. The TFIID component TAF(II)130 potentiates STAT2 function, but TAF(II)28 or the HAT activity of TAF(II)250 do not, and transcriptional induction can proceed independently of the TATA-binding protein, TBP. Moreover, IFN-stimulated transcription was resistant to poliovirus-targeted degradation by TBP, and continued despite host-cell transcriptional shutoff during poliovirus infection. We conclude that a non-classical transcriptional mechanism combats an anticellular action of poliovirus, through a TBP-free TAF-containing complex and GCN5.
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PMID:IFN-Stimulated transcription through a TBP-free acetyltransferase complex escapes viral shutoff. 1180 63

General transcription factor TFIID is a key component of RNA polymerase II transcription initiation. Human TFIID is a megadalton-sized complex comprising TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs). TBP binds to core promoter DNA, recognizing the TATA-box. We identified a ternary complex formed by TBP and the histone fold (HF) domain-containing TFIID subunits TAF11 and TAF13. We demonstrate that TAF11/TAF13 competes for TBP binding with TATA-box DNA, and also with the N-terminal domain of TAF1 previously implicated in TATA-box mimicry. In an integrative approach combining crystal coordinates, biochemical analyses and data from cross-linking mass-spectrometry (CLMS), we determine the architecture of the TAF11/TAF13/TBP complex, revealing TAF11/TAF13 interaction with the DNA binding surface of TBP. We identify a highly conserved C-terminal TBP-interaction domain (CTID) in TAF13, which is essential for supporting cell growth. Our results thus have implications for cellular TFIID assembly and suggest a novel regulatory state for TFIID function.
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PMID:Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID. 2911 74