Disease relevance of TAF7

• Decreased TAF7 expression, by RNA interference, in androgen-independent human prostate cancer LN-CaP104-R1 cells resulted in lower polyamine transport activity (25% of control) and resistance to MGBG-induced growth arrest [1].

High impact information on TAF7

• Chromatin immunoprecipitation analyses using the DPE-dependent IRF-1 and TAF7 promoters demonstrated that CK2, and PC4 are present on these promoters in vivo [2].
• The present study has focused on the role of the TFIID component, TAF7, in regulating transcription initiation [3].
• TAF(II)55 binding to TAF(II)250 inhibits its AT activity [4].
• These results strongly suggest that the TAF(II)55 interactions with the modified RXR LBDs modulate transcriptional activation [5].
• We have identified novel interactions between the human (h)TATA-binding protein-associated factor TAF(II)55 and the ligand-binding domains (LBDs) of the nuclear receptors for vitamin D(3) (VDR) and thyroid hormone (TRalpha) [5].

Biological context of TAF7

• Interaction in vitro correlates with enhanced transactivation function of c-Jun in HEK293 and COS cells in the presence of increasing amounts of TAF7 [6].
• Taken together, these results reveal a physiological function of TAF7 as a basal regulator for mammalian polyamine transport activity and MGBG-induced apoptosis [1].
• To uncover the regulatory properties of the general transcription machinery, we have isolated the hTAF(II)55 gene and dissected the regulatory elements and the core promoter responsible for hTAF(II)55 gene expression [7].
• Surprisingly, the hTAF(II)55 gene has a single uninterrupted open reading frame and is the only intronless general transcription factor identified so far [7].
• The ptr6(+) gene was found to encode an essential protein of 393 amino acids, which shares significant homology in amino acid sequence with yTAFII67 of budding yeast Saccharomyces cerevisiae and human hTAFII55, a subunit of the general transcription factor complex TFIID [8].

Anatomical context of TAF7

• TAF7-deficient cells had decreased capacity for polyamine uptake (20% of CHO cells), decreased AP-1 activation, as well as resistance to MGBG-induced apoptosis [1].
• This provides us with an estimation of the in vivo half-lives of TBP and TAFII55, which were assessed to be less than 20 and 6 hours, respectively, in HeLa cells [9].

Associations of TAF7 with chemical compounds

• Human TAF(II)55 interacts with the vitamin D(3) and thyroid hormone receptors and with derivatives of the retinoid X receptor that have altered transactivation properties [5].

Physical interactions of TAF7

• Multiple interactions between hTAFII55 and other TFIID subunits. Requirements for the formation of stable ternary complexes between hTAFII55 and the TATA-binding protein [10].

Regulatory relationships of TAF7

• Thus, TAF(II)55 is capable of regulating TAF(II)250 function by modulating its AT activity [4].

Other interactions of TAF7

• We further show that purified recombinant TIF1alpha possesses intrinsic kinase activity and that, in addition to autophosphorylation, TIF1alpha selectively phosphorylates the transcription factors TFIIEalpha, TAFII28, and TAFII55 in vitro [11].

References