Summary: Transcription initiation factor TFIID component TAF4 family
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|TAF4 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 135kDa|
PDB rendering based on 1h3o.
|RNA expression pattern|
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.
crystal structure of the human taf4-taf12 (tafii135-tafii20) complex
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.
- Tanese N, Saluja D, Vassallo MF, Chen JL, Admon A (January 1997). "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. doi:10.1073/pnas.93.24.13611. PMC 19367. PMID 8942982.
- Mengus G, May M, Carre L, Chambon P, Davidson I (July 1997). "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. doi:10.1101/gad.11.11.1381. PMID 9192867.
- "Entrez Gene: TAF4 TAF4 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 135kDa".
- Pointud, Jean-Christophe; Mengus Gabrielle, Brancorsini Stefano, Monaco Lucia, Parvinen Martti, Sassone-Corsi Paolo, Davidson Irwin (May 2003). "The intracellular localisation of TAF7L, a paralogue of transcription factor TFIID subunit TAF7, is developmentally regulated during male germ-cell differentiation". J. Cell. Sci. (England) 116 (Pt 9): 1847–58. doi:10.1242/jcs.00391. ISSN 0021-9533. PMID 12665565.
- Bellorini, M; Lee D K, Dantonel J C, Zemzoumi K, Roeder R G, 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 Res. (ENGLAND) 25 (11): 2174–81. doi:10.1093/nar/25.11.2174. ISSN 0305-1048. PMC 146709. PMID 9153318.
- Vassallo, Milo F; Tanese Naoko (April 2002). "Isoform-specific interaction of HP1 with human TAFII130". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (9): 5919–24. doi:10.1073/pnas.092025499. ISSN 0027-8424. PMC 122877. PMID 11959914.
- Brand, M; Moggs J G, Oulad-Abdelghani M, Lejeune F, Dilworth F J, Stevenin J, Almouzni G, Tora L (June 2001). "UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation". EMBO J. (England) 20 (12): 3187–96. doi:10.1093/emboj/20.12.3187. ISSN 0261-4189. PMC 150203. PMID 11406595.
- Thuault S, Gangloff YG, Kirchner J, Sanders S, Werten S, Romier C, Weil PA, Davidson I (November 2002). "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. doi:10.1074/jbc.M206556200. PMID 12237303.
- Zhou Q, Sharp PA (1995). "Novel mechanism and factor for regulation by HIV-1 Tat.". EMBO J. 14 (2): 321–8. PMC 398086. PMID 7835343.
- Parada CA, Yoon JB, Roeder RG (1995). "A novel LBP-1-mediated restriction of HIV-1 transcription at the level of elongation in vitro.". J. Biol. Chem. 270 (5): 2274–83. doi:10.1074/jbc.270.5.2274. PMID 7836461.
- Ou SH, Garcia-Martínez LF, Paulssen EJ, Gaynor RB (1994). "Role of flanking E box motifs in human immunodeficiency virus type 1 TATA element function.". J. Virol. 68 (11): 7188–99. PMC 237158. PMID 7933101.
- Kashanchi F, Piras G, Radonovich MF, et al. (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, et al. (1996). "Wild-type and transactivation-defective mutants of human immunodeficiency virus type 1 Tat protein bind human TATA-binding protein in vitro.". J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 12 (2): 128–38. doi:10.1097/00042560-199606010-00005. PMID 8680883.
- Pendergrast PS, Morrison D, Tansey WP, Hernandez N (1996). "Mutations in the carboxy-terminal domain of TBP affect the synthesis of human immunodeficiency virus type 1 full-length and short transcripts similarly.". J. Virol. 70 (8): 5025–34. PMC 190456. PMID 8764009.
- Kashanchi F, Khleif SN, Duvall JF, et al. (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.". J. Virol. 70 (8): 5503–10. PMC 190508. PMID 8764062.
- Zhou Q, Sharp PA (1996). "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat.". Science 274 (5287): 605–10. doi:10.1126/science.274.5287.605. PMID 8849451.
- García-Martínez LF, Ivanov D, Gaynor RB (1997). "Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes.". J. Biol. Chem. 272 (11): 6951–8. doi:10.1074/jbc.272.11.6951. PMID 9054383.
- Saluja D, Vassallo MF, Tanese N (1998). "Distinct subdomains of human TAFII130 are required for interactions with glutamine-rich transcriptional activators.". Mol. Cell. Biol. 18 (10): 5734–43. PMC 109159. PMID 9742090.
- Brand M, Yamamoto K, Staub A, Tora L (1999). "Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction.". J. Biol. Chem. 274 (26): 18285–9. doi:10.1074/jbc.274.26.18285. PMID 10373431.
- Inada A, Someya Y, Yamada Y, et al. (1999). "The cyclic AMP response element modulator family regulates the insulin gene transcription by interacting with transcription factor IID.". J. Biol. Chem. 274 (30): 21095–103. doi:10.1074/jbc.274.30.21095. PMID 10409662.
- Gangloff YG, Werten S, Romier C, et al. (2000). "The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs.". Mol. Cell. Biol. 20 (1): 340–51. doi:10.1128/MCB.20.1.340-351.2000. PMC 85089. PMID 10594036.
- Brand M, Moggs JG, Oulad-Abdelghani M, et al. (2001). "UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation.". EMBO J. 20 (12): 3187–96. doi:10.1093/emboj/20.12.3187. PMC 150203. PMID 11406595.
- Martinez E, Palhan VB, Tjernberg A, et al. (2001). "Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo.". Mol. Cell. Biol. 21 (20): 6782–95. doi:10.1128/MCB.21.20.6782-6795.2001. PMC 99856. PMID 11564863.
- Guermah M, Tao Y, Roeder RG (2001). "Positive and negative TAF(II) functions that suggest a dynamic TFIID structure and elicit synergy with traps in activator-induced transcription.". Mol. Cell. Biol. 21 (20): 6882–94. doi:10.1128/MCB.21.20.6882-6894.2001. PMC 99865. PMID 11564872.
- Felinski EA, Quinn PG (2001). "The coactivator dTAF(II)110/hTAF(II)135 is sufficient to recruit a polymerase complex and activate basal transcription mediated by CREB.". Proc. Natl. Acad. Sci. U.S.A. 98 (23): 13078–83. doi:10.1073/pnas.241337698. PMC 60827. PMID 11687654.
- Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
|This article on a gene on chromosome 20 is a stub. You can help Wikipedia by expanding it.|
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Transcription initiation factor TFIID component TAF4 family Provide feedback
This region of similarity is found in Transcription initiation factor TFIID component TAF4 .
Thuault S, Gangloff YG, Kirchner J, Sanders S, Werten S, Romier C, Weil PA, Davidson I; , J Biol Chem 2002;277:45510-45517.: Functional analysis of the TFIID-specific yeast TAF4 (yTAF(II)48) reveals an unexpected organization of its histone-fold domain. PUBMED:12237303 EPMC:12237303
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR007900
Accurate transcription initiation at protein-coding genes by RNA polymerase II requires the assembly of a multiprotein complex around the mRNA start site. Transcription factor TFIID is one of the general factors involved in this process. Yeast TFIID comprises the TATA binding protein and 14 TBP-associated factors (TAFIIs), nine of which contain histone-fold domains. 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 [PUBMED:12237303].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||transcription factor TFIID complex (GO:0005669)|
|Biological process||transcription initiation, DNA-dependent (GO:0006352)|
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|Seed source:||Wood V|
|Number in seed:||26|
|Number in full:||410|
|Average length of the domain:||237.20 aa|
|Average identity of full alignment:||28 %|
|Average coverage of the sequence by the domain:||39.18 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||9|
|Download:||download the raw HMM for this family|
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For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the TAF4 domain has been found. There are 2 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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