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TAF11  -  TAF11 RNA polymerase II, TATA box binding...

Homo sapiens

Synonyms: MGC:15243, PRO2134, TAF(II)28, TAF2I, TAFII-28, ...
 
 
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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

  1. Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family. Birck, C., Poch, O., Romier, C., Ruff, M., Mengus, G., Lavigne, A.C., Davidson, I., Moras, D. Cell (1998) [Pubmed]
  2. Human TAF(II28) promotes transcriptional stimulation by activation function 2 of the retinoid X receptors. May, M., Mengus, G., Lavigne, A.C., Chambon, P., Davidson, I. EMBO J. (1996) [Pubmed]
  3. Genomics and transcription analysis of human TFIID. Purrello, M., Di Pietro, C., Viola, A., Rapisarda, A., Stevens, S., Guermah, M., Tao, Y., Bonaiuto, C., Arcidiacono, A., Messina, A., Sichel, G., Grzeschik, K.H., Roeder, R. Oncogene (1998) [Pubmed]
  4. Human TAF(II)28 interacts with the human T cell leukemia virus type I Tax transactivator and promotes its transcriptional activity. Caron, C., Mengus, G., Dubrowskaya, V., Roisin, A., Davidson, I., Jalinot, P. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  5. Synergistic transcriptional activation by TATA-binding protein and hTAFII28 requires specific amino acids of the hTAFII28 histone fold. Lavigne, A.C., Gangloff, Y.G., Carré, L., Mengus, G., Birck, C., Poch, O., Romier, C., Moras, D., Davidson, I. Mol. Cell. Biol. (1999) [Pubmed]
  6. 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. Mengus, G., Gangloff, Y.G., Carré, L., Lavigne, A.C., Davidson, I. J. Biol. Chem. (2000) [Pubmed]
  7. Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID. Mengus, G., May, M., Jacq, X., Staub, A., Tora, L., Chambon, P., Davidson, I. EMBO J. (1995) [Pubmed]
  8. The putative cofactor TIF1alpha is a protein kinase that is hyperphosphorylated upon interaction with liganded nuclear receptors. Fraser, R.A., Heard, D.J., Adam, S., Lavigne, A.C., Le Douarin, B., Tora, L., Losson, R., Rochette-Egly, C., Chambon, P. J. Biol. Chem. (1998) [Pubmed]
  9. The TATA-binding protein and its associated factors are differentially expressed in adult mouse tissues. Perletti, L., Dantonel, J.C., Davidson, I. J. Biol. Chem. (1999) [Pubmed]
 
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