TAF7

Transcription initiation factor TFIID subunit 7 also known as TAFII55 is a protein that in humans is encoded by the TAF7 gene.[5]

TAF7
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4RGW, 5FUR
Identifiers
Aliases	TAF7, TAF2F, TAFII55, TATA-box binding protein associated factor 7
External IDs	OMIM: 600573 MGI: 1346348 HomoloGene: 133942 GeneCards: TAF7
Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5q31.3 Start 141,260,225 bp[1] End 141,320,784 bp[1]
Gene location (Mouse) Chr. Chromosome 18 (mouse)[2] Band 18|18 B3 Start 37,640,491 bp[2] End 37,644,204 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity • GO:0001105 transcription coactivator activity • transcription factor binding • thyroid hormone receptor binding • GO:0001948 protein binding • histone acetyltransferase binding • vitamin D receptor binding • protein heterodimerization activity • H3K27me3 modified histone binding • TFIIH-class transcription factor binding • P-TEFb complex binding Cellular component • cytoplasm • Golgi apparatus • transcription factor TFTC complex • MLL1 complex • cyclin/CDK positive transcription elongation factor complex • cell nucleus • nucleoplasm • transcription factor complex • transcription factor TFIID complex Biological process • regulation of transcription, DNA-templated • negative regulation of protein kinase activity • regulation of transcription from RNA polymerase II promoter • spermine transport • RNA polymerase II transcriptional preinitiation complex assembly • negative regulation of transcription from RNA polymerase II promoter • transcription, DNA-templated • DNA-templated transcription, initiation • negative regulation of transcription, DNA-templated • negative regulation of histone acetylation • intracellular estrogen receptor signaling pathway • positive regulation of transcription from RNA polymerase II promoter • transcription from RNA polymerase II promoter • transcription initiation from RNA polymerase II promoter • regulation of transcription initiation from RNA polymerase II promoter • regulation of signal transduction by p53 class mediator Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6879	24074
Ensembl	ENSG00000178913	ENSMUSG00000051316
UniProt	Q15545	Q9R1C0
RefSeq (mRNA)	NM_005642	NM_175770
RefSeq (protein)	NP_005633	NP_786964
Location (UCSC)	Chr 5: 141.26 – 141.32 Mb	Chr 18: 37.64 – 37.64 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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.[6]

TAFII55_N
Identifiers
Symbol	TAFII55_N
Pfam	PF04658
InterPro	IPR006751
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

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.[7] The conserved region is situated towards the N-terminal of the protein.[8] 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, it is 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[9]

Interactions

TAF7 has been shown to interact with:

• TAF15,[10]
• TAF1,[8] and
• TATA binding protein.[11][12]

References

1. GRCh38: Ensembl release 89: ENSG00000178913 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000051316 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: TAF7 TAF7 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 55kDa".
7. 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.
8. 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.
9. 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.
10. 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.
11. 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.
12. 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.

Further reading

• Zhou Q, Sharp PA (January 1995). "Novel mechanism and factor for regulation by HIV-1 Tat". The EMBO Journal. 14 (2): 321–8. doi:10.1002/j.1460-2075.1995.tb07006.x. PMC 398086. PMID 7835343.
• Parada CA, Yoon JB, Roeder RG (February 1995). "A novel LBP-1-mediated restriction of HIV-1 transcription at the level of elongation in vitro". The Journal of Biological Chemistry. 270 (5): 2274–83. doi:10.1074/jbc.270.5.2274. PMID 7836461.
• Ou SH, Garcia-Martínez LF, Paulssen EJ, Gaynor RB (November 1994). "Role of flanking E box motifs in human immunodeficiency virus type 1 TATA element function". Journal of Virology. 68 (11): 7188–99. doi:10.1128/JVI.68.11.7188-7199.1994. PMC 237158. PMID 7933101.
• Cross SH, Charlton JA, Nan X, Bird AP (March 1994). "Purification of CpG islands using a methylated DNA binding column". Nature Genetics. 6 (3): 236–44. doi:10.1038/ng0394-236. PMID 8012384.
• Kashanchi F, Piras G, Radonovich MF, Duvall JF, Fattaey A, Chiang CM, Roeder RG, Brady JN (January 1994). "Direct interaction of human TFIID with the HIV-1 transactivator tat". Nature. 367 (6460): 295–9. doi:10.1038/367295a0. PMID 8121496.
• Wang Z, Morris GF, Rice AP, Xiong W, Morris CB (June 1996). "Wild-type and transactivation-defective mutants of human immunodeficiency virus type 1 Tat protein bind human TATA-binding protein in vitro". Journal of Acquired Immune Deficiency Syndromes and Human Retrovirology. 12 (2): 128–38. doi:10.1097/00042560-199606010-00005. PMID 8680883.
• Lavigne AC, Mengus G, May M, Dubrovskaya V, Tora L, Chambon P, Davidson I (August 1996). "Multiple interactions between hTAFII55 and other TFIID subunits. Requirements for the formation of stable ternary complexes between hTAFII55 and the TATA-binding protein". The Journal of Biological Chemistry. 271 (33): 19774–80. doi:10.1074/jbc.271.33.19774. PMID 8702684.
• Pendergrast PS, Morrison D, Tansey WP, Hernandez N (August 1996). "Mutations in the carboxy-terminal domain of TBP affect the synthesis of human immunodeficiency virus type 1 full-length and short transcripts similarly". Journal of Virology. 70 (8): 5025–34. doi:10.1128/JVI.70.8.5025-5034.1996. PMC 190456. PMID 8764009.
• Kashanchi F, Khleif SN, Duvall JF, Sadaie MR, Radonovich MF, Cho M, Martin MA, Chen SY, Weinmann R, Brady JN (August 1996). "Interaction of human immunodeficiency virus type 1 Tat with a unique site of TFIID inhibits negative cofactor Dr1 and stabilizes the TFIID-TFIIA complex". Journal of Virology. 70 (8): 5503–10. doi:10.1128/JVI.70.8.5503-5510.1996. PMC 190508. PMID 8764062.
• Rowlands JC, McEwan IJ, Gustafsson JA (September 1996). "Trans-activation by the human aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator proteins: direct interactions with basal transcription factors". Molecular Pharmacology. 50 (3): 538–48. PMID 8794892.
• Zhou Q, Sharp PA (October 1996). "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat". Science. 274 (5287): 605–10. Bibcode:1996Sci...274..605Z. doi:10.1126/science.274.5287.605. PMID 8849451.
• García-Martínez LF, Ivanov D, Gaynor RB (March 1997). "Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes". The Journal of Biological Chemistry. 272 (11): 6951–8. doi:10.1074/jbc.272.11.6951. PMID 9054383.
• Dantonel JC, Murthy KG, Manley JL, Tora L (September 1997). "Transcription factor TFIID recruits factor CPSF for formation of 3' end of mRNA". Nature. 389 (6649): 399–402. doi:10.1038/38763. PMID 9311784.
• 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.
• Fraser RA, Heard DJ, Adam S, Lavigne AC, Le Douarin B, Tora L, Losson R, Rochette-Egly C, Chambon P (June 1998). "The putative cofactor TIF1alpha is a protein kinase that is hyperphosphorylated upon interaction with liganded nuclear receptors". The Journal of Biological Chemistry. 273 (26): 16199–204. doi:10.1074/jbc.273.26.16199. PMID 9632676.
• Furukawa T, Tanese N (September 2000). "Assembly of partial TFIID complexes in mammalian cells reveals distinct activities associated with individual TATA box-binding protein-associated factors". The Journal of Biological Chemistry. 275 (38): 29847–56. doi:10.1074/jbc.M002989200. PMID 10896937.
• Yuan CX, Gurley WB (July 2000). "Potential targets for HSF1 within the preinitiation complex". Cell Stress & Chaperones. 5 (3): 229–42. doi:10.1379/1466-1268(2000)005<0229:PTFHWT>2.0.CO;2. PMC 312889. PMID 11005381.
• Wu Q, Zhang T, Cheng JF, Kim Y, Grimwood J, Schmutz J, Dickson M, Noonan JP, Zhang MQ, Myers RM, Maniatis T (March 2001). "Comparative DNA sequence analysis of mouse and human protocadherin gene clusters". Genome Research. 11 (3): 389–404. doi:10.1101/gr.167301. PMC 311048. PMID 11230163.
• Zhou T, Chiang CM (July 2001). "The intronless and TATA-less human TAF(II)55 gene contains a functional initiator and a downstream promoter element". The Journal of Biological Chemistry. 276 (27): 25503–11. doi:10.1074/jbc.M102875200. PMID 11340078.

External links

• FactorBook TAF7
• Overview of all the structural information available in the PDB for UniProt: Q15545 (Transcription initiation factor TFIID subunit 7) at the PDBe-KB.