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Transcription initiation factor TFIID subunit 7 also known as TAFII55 is a protein that in humans is encoded by the TAF7 gene.[1]


The intronless gene for this transcription coactivator is located between the protocadherin beta and gamma gene clusters on chromosome 5. The protein encoded by this gene is a component of the TFIID protein complex, a complex which binds to the TATA box in class II promoters and recruits RNA polymerase II and other factors. This particular subunit interacts with the largest TFIID subunit, as well as multiple transcription activators. The protein is required for transcription by promoters targeted by RNA polymerase II.[2]


The general transcription factor, TFIID, consists of the TATA-binding protein (TBP) associated with a series of TBP-associated factors (TAFs) that together participate in the assembly of the transcription preinitiation complex. TAFII55 binds to TAFII250 and inhibits its acetyltransferase activity. The exact role of TAFII55 is currently unknown but studies have shown that it interacts with the C-jun pathway.[3] The conserved region is situated towards the N-terminal of the protein.[4] This entry talks about the N-terminal domain.

Crystallographic studies have revealed a very significant hydrophobic pocket between TAF7 and TAF1, its main binding partner. Due to the incredible hydrophobicity of this interaction, its unlikely that TAF1 would be able to fold properly without the presence of TAF7. Thus, it is possible that TAF7 is required for proper production of TAF1[5]


TAF7 has been shown to interact with:


  1. Chiang CM, Roeder RG (January 1995). "Cloning of an intrinsic human TFIID subunit that interacts with multiple transcriptional activators". Science. 267 (5197): 531–6. doi:10.1126/science.7824954. PMID 7824954.
  2. "Entrez Gene: TAF7 TAF7 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 55kDa".
  3. Munz C, Psichari E, Mandilis D, Lavigne AC, Spiliotaki M, Oehler T, Davidson I, Tora L, Angel P, Pintzas A (June 2003). "TAF7 (TAFII55) plays a role in the transcription activation by c-Jun". The Journal of Biological Chemistry. 278 (24): 21510–6. doi:10.1074/jbc.M212764200. PMID 12676957.
  4. 4.0 4.1 Gegonne A, Weissman JD, Singer DS (October 2001). "TAFII55 binding to TAFII250 inhibits its acetyltransferase activity". Proceedings of the National Academy of Sciences of the United States of America. 98 (22): 12432–7. doi:10.1073/pnas.211444798. PMC 60071. PMID 11592977.
  5. Bhattacharya S, Lou X, Hwang P, Rajashankar KR, Wang X, Gustafsson JÅ, Fletterick RJ, Jacobson RH, Webb P (June 2014). "Structural and functional insight into TAF1-TAF7, a subcomplex of transcription factor II D". Proceedings of the National Academy of Sciences of the United States of America. 111 (25): 9103–8. doi:10.1073/pnas.1408293111. PMC 4078864. PMID 24927529.
  6. Bertolotti A, Melot T, Acker J, Vigneron M, Delattre O, Tora L (March 1998). "EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes". Molecular and Cellular Biology. 18 (3): 1489–97. doi:10.1128/mcb.18.3.1489. PMC 108863. PMID 9488465.
  7. Pointud JC, Mengus G, Brancorsini S, Monaco L, Parvinen M, Sassone-Corsi P, Davidson I (May 2003). "The intracellular localisation of TAF7L, a paralogue of transcription factor TFIID subunit TAF7, is developmentally regulated during male germ-cell differentiation". Journal of Cell Science. 116 (Pt 9): 1847–58. doi:10.1242/jcs.00391. PMID 12665565.
  8. Bellorini M, Lee DK, Dantonel JC, Zemzoumi K, Roeder RG, Tora L, Mantovani R (June 1997). "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 Research. 25 (11): 2174–81. doi:10.1093/nar/25.11.2174. PMC 146709. PMID 9153318.

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