TAF4 explained

Transcription initiation factor TFIID subunit 4 is a protein that in humans is encoded by the TAF4 gene.[1] [2] [3]

Function

Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes one of the larger subunits of TFIID that has been shown to potentiate transcriptional activation by retinoic acid, thyroid hormone and vitamin D3 receptors. In addition, this subunit interacts with the transcription factor CREB, which has a glutamine-rich activation domain, and binds to other proteins containing glutamine-rich regions. Aberrant binding to this subunit by proteins with expanded polyglutamine regions has been suggested as one of the pathogenetic mechanisms underlying a group of neurodegenerative disorders referred to as polyglutamine diseases.

Interactions

TAF4 has been shown to interact with:

Protein domain

Symbol:TAF4
TAF4
Pfam:PF05236
Interpro:IPR007900
Scop:1h3o

Yeast TFIID comprises the TATA binding protein and 14 TBP-associated factors (TAFIIs), nine of which contain histone-fold domains (INTERPRO). The C-terminal region of the TFIID-specific yeast TAF4 (yTAF4) containing the HFD shares strong sequence similarity with Drosophila (d)TAF4 and human TAF4. A structure/function analysis of yTAF4 demonstrates that the HFD, a short conserved C-terminal domain (CCTD), and the region separating them are all required for yTAF4 function. This region of similarity is found in Transcription initiation factor TFIID component TAF4.[8]

Further reading

Notes and References

  1. Tanese N, Saluja D, Vassallo MF, Chen JL, Admon A . Molecular cloning and analysis of two subunits of the human TFIID complex: hTAFII130 and hTAFII100 . Proc. Natl. Acad. Sci. U.S.A. . 93 . 24 . 13611–6 . 1996 . 8942982 . 19367 . 10.1073/pnas.93.24.13611 . 1996PNAS...9313611T . free .
  2. Mengus G, May M, Carré L, Chambon P, Davidson I . Human TAF(II)135 potentiates transcriptional activation by the AF-2s of the retinoic acid, vitamin D3, and thyroid hormone receptors in mammalian cells . Genes Dev. . 11 . 11 . 1381–95 . July 1997 . 9192867 . 10.1101/gad.11.11.1381 . free .
  3. Web site: Entrez Gene: TAF4 TAF4 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 135kDa.
  4. Vassallo MF, Tanese N . Isoform-specific interaction of HP1 with human TAFII130 . Proc. Natl. Acad. Sci. U.S.A. . 99 . 9 . 5919–24 . April 2002 . 11959914 . 122877 . 10.1073/pnas.092025499 . 2002PNAS...99.5919V . free .
  5. Pointud JC, Mengus G, Brancorsini S, Monaco L, Parvinen M, Sassone-Corsi P, Davidson I . The intracellular localisation of TAF7L, a paralogue of transcription factor TFIID subunit TAF7, is developmentally regulated during male germ-cell differentiation . J. Cell Sci. . 116 . Pt 9 . 1847–58 . May 2003 . 12665565 . 10.1242/jcs.00391. free .
  6. Bellorini M, Lee DK, Dantonel JC, Zemzoumi K, Roeder RG, Tora L, Mantovani R . CCAAT binding NF-Y-TBP interactions: NF-YB and NF-YC require short domains adjacent to their histone fold motifs for association with TBP basic residues . Nucleic Acids Res. . 25 . 11 . 2174–81 . June 1997 . 9153318 . 146709 . 10.1093/nar/25.11.2174.
  7. Brand M, Moggs JG, Oulad-Abdelghani M, Lejeune F, Dilworth FJ, Stevenin J, Almouzni G, Tora L . UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation . EMBO J. . 20 . 12 . 3187–96 . June 2001 . 11406595 . 150203 . 10.1093/emboj/20.12.3187 .
  8. Thuault S, Gangloff YG, Kirchner J, Sanders S, Werten S, Romier C, Weil PA, Davidson I . Functional analysis of the TFIID-specific yeast TAF4 (yTAF(II)48) reveals an unexpected organization of its histone-fold domain . J. Biol. Chem. . 277 . 47 . 45510–7 . November 2002 . 12237303 . 10.1074/jbc.M206556200 . free .