High impact information on TAF11

• The histone folds in hTAF(II)28 and hTAF(II)18 were not predicted from their primary sequence, indicating that these TAF(II)s define a novel family of atypical histone fold sequences [1].
• In agreement with these data, showing that TAF(II)28 is limiting in the AF-2 activation pathway in Cos cells, TAF(II)28 is selectively depleted in Cos cell TFIID [2].
• The expression of hTAF(II)28 also potentiated transactivation by several nuclear receptors, notably the oestrogen and vitamin D3 receptors (ER and VDR), whereas other classes of activator were not affected [2].
• In contrast to Cos cells, the RXR AF-2s had differential abilities to activate transcription from a minimal promoter in HeLa cells, and a lesser increase in their activity was observed upon hTAFII28 coexpression [2].
• However, coexpression of human (h) TAF(II)28 promotes a strong ligand-dependent activity of the RXR AF-2 on a minimal promoter and potentiates the ability of the RXRalpha AF-2 to activate transcription from a complex promoter [2].

Biological context of TAF11

• Except for those encoding TAF(II)250 and TAF(II)31, these genes are present in a single copy and, with the exclusion of those for TAF(II)43 and TAF(II)28 (both at 6p21), are localized in different segments of the genome [3].

Anatomical context of TAF11

• Human TAF(II)28 interacts with the human T cell leukemia virus type I Tax transactivator and promotes its transcriptional activity [4].

Associations of TAF11 with chemical compounds

• Coexpression of the human TATA-binding protein (TBP)-associated factor 28 (hTAFII28) with the altered-specificity mutant TBP spm3 synergistically enhances transcriptional activation by the activation function 2 of the nuclear receptors (NRs) for estrogen and vitamin D3 from a reporter plasmid containing a TGTA element in mammalian cells [5].
• 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) [6].

Other interactions of TAF11

• The binding of hTAFII28 and hTAFII30 requires distinct domains of hTAFII18 [7].
• 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 [8].
• While there are significant variations in the levels of TAFII28 protein, reverse transcription-coupled polymerase chain reaction shows similar expression of the TAFII28 mRNA in different tissues [9].

References