Summary: Transcription factor TFIID (or TATA-binding protein, TBP)
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TATA-binding protein Edit Wikipedia article
|, GTF2D, GTF2D1, HDL4, SCA17, TFIID, TATA-box binding protein, TATA-binding protein|
|RNA expression pattern|
|View/Edit Human||View/Edit Mouse|
crystal structure of a yeast brf1-tbp-dna ternary complex
The TATA-binding protein (TBP) is a general transcription factor that binds specifically to a DNA sequence called the TATA box. This DNA sequence is found about 30 base pairs upstream of the transcription start site in some eukaryotic gene promoters. TBP, along with a variety of TBP-associated factors, make up the TFIID, a general transcription factor that in turn makes up part of the RNA polymerase II preinitiation complex. As one of the few proteins in the preinitiation complex that binds DNA in a sequence-specific manner, it helps position RNA polymerase II over the transcription start site of the gene. However, it is estimated that only 10–20% of human promoters have TATA boxes. Therefore, TBP is probably not the only protein involved in positioning RNA polymerase II.
TBP is involved in DNA melting (double strand separation) by bending the DNA by 80° (the AT-rich sequence to which it binds facilitates easy melting). The TBP is an unusual protein in that it binds the minor groove using a β sheet.
Another distinctive feature of TBP is a long string of glutamines in the N-terminus of the protein. This region modulates the DNA binding activity of the C-terminus, and modulation of DNA-binding affects the rate of transcription complex formation and initiation of transcription. Mutations that expand the number of CAG repeats encoding this polyglutamine tract, and thus increase the length of the polyglutamine string, are associated with spinocerebellar ataxia 17, a neurodegenerative disorder classified as a polyglutamine disease.
Role as transcription factor
TBP is a subunit of the eukaryotic transcription factor TFIID. TFIID is the first protein to bind to DNA during the formation of the pre-initiation transcription complex of RNA polymerase II (RNA Pol II). Binding of TFIID to the TATA box in the promoter region of the gene initiates the recruitment of other factors required for RNA Pol II to begin transcription. Some of the other recruited transcription factors include TFIIA, TFIIB, and TFIIF. Each of these transcription factors is formed from the interaction of many protein subunits, indicating that transcription is a heavily regulated process.
TBP is also a component of RNA polymerase I and RNA polymerase III and is therefore involved in transcription initiation by all three RNA polymerases. In specific cell types or on specific promoters TBP can be replaced by one of several TBP-related factors.
When TBP binds to a TATA box within the DNA, it distorts the DNA by inserting amino acid side-chains between base pairs, partially unwinding the helix, and doubly kinking it. The distortion is accomplished through a great amount of surface contact between the protein and DNA. TBP binds with the negatively charged phosphates in the DNA backbone through positively charged lysine and arginine amino acid residues. The sharp bend in the DNA is produced through projection of four bulky phenylalanine residues into the minor groove. As the DNA bends, its contact with TBP increases, thus enhancing the DNA-protein interaction.
The strain imposed on the DNA through this interaction initiates melting, or separation, of the strands. Because this region of DNA is rich in adenine and thymine residues, which base-pair through only two hydrogen bonds, the DNA strands are more easily separated. Separation of the two strands exposes the bases and allows RNA polymerase II to begin transcription of the gene.
TBP's C-terminus composes of a helicoidal shape that (incompletely) complements the T-A-T-A region of DNA. It is interesting to note that this incompleteness allows DNA to be passively bent on binding.
TATA-binding protein has been shown to interact with:
- GTF2B (TFIIB),
- GTF2A1 (TFIIA subunit 1),
- GTF2F1 (TFIIF subunit 1)
- GTF2H4 (TFIIH subunit 4),
- TAF13, and
The TATA-box binding protein (TBP) is required for the initiation of transcription by RNA polymerases I, II and III, from promoters with or without a TATA box. In the presence of a TATA-less box promoter the TBP binds with the help of TAF250 &150. TBP associates with a host of factors, including the general transcription factors TFIIA, -B, -D, -E, and -H, to form huge multi-subunit pre-initiation complexes on the core promoter. Through its association with different transcription factors, TBP can initiate transcription from different RNA polymerases. There are several related TBPs, including TBP-like (TBPL) proteins.
The C-terminal core of TBP (~180 residues) is highly conserved and contains two 88-amino acid repeats that produce a saddle-shaped structure that straddles the DNA; this region binds to the TATA box and interacts with transcription factors and regulatory proteins . By contrast, the N-terminal region varies in both length and sequence.
- "Human PubMed Reference:".
- "Mouse PubMed Reference:".
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- Bushnell DA, Westover KD, Davis RE, Kornberg RD (February 2004). "Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms". Science. 303 (5660): 983–8. doi:10.1126/science.1090838. PMID 14963322.
- DeJong J, Bernstein R, Roeder RG (April 1995). "Human general transcription factor TFIIA: characterization of a cDNA encoding the small subunit and requirement for basal and activated transcription". Proc. Natl. Acad. Sci. U.S.A. 92 (8): 3313–7. doi:10.1073/pnas.92.8.3313. PMC . PMID 7724559.
- Ozer J, Mitsouras K, Zerby D, Carey M, Lieberman PM (June 1998). "Transcription factor IIA derepresses TATA-binding protein (TBP)-associated factor inhibition of TBP-DNA binding". J. Biol. Chem. 273 (23): 14293–300. doi:10.1074/jbc.273.23.14293. PMID 9603936.
- Sun X, Ma D, Sheldon M, Yeung K, Reinberg D (October 1994). "Reconstitution of human TFIIA activity from recombinant polypeptides: a role in TFIID-mediated transcription". Genes Dev. 8 (19): 2336–48. doi:10.1101/gad.8.19.2336. PMID 7958900.
- Ruppert S, Tjian R (November 1995). "Human TAFII250 interacts with RAP74: implications for RNA polymerase II initiation". Genes Dev. 9 (22): 2747–55. doi:10.1101/gad.9.22.2747. PMID 7590250.
- Malik S, Guermah M, Roeder RG (March 1998). "A dynamic model for PC4 coactivator function in RNA polymerase II transcription". Proc. Natl. Acad. Sci. U.S.A. 95 (5): 2192–7. doi:10.1073/pnas.95.5.2192. PMC . PMID 9482861.
- Thut CJ, Goodrich JA, Tjian R (August 1997). "Repression of p53-mediated transcription by MDM2: a dual mechanism". Genes Dev. 11 (15): 1974–86. doi:10.1101/gad.11.15.1974. PMC . PMID 9271120.
- Léveillard T, Wasylyk B (December 1997). "The MDM2 C-terminal region binds to TAFII250 and is required for MDM2 regulation of the cyclin A promoter". J. Biol. Chem. 272 (49): 30651–61. doi:10.1074/jbc.272.49.30651. PMID 9388200.
- Shetty S, Takahashi T, Matsui H, Ayengar R, Raghow R (May 1999). "Transcriptional autorepression of Msx1 gene is mediated by interactions of Msx1 protein with a multi-protein transcriptional complex containing TATA-binding protein, Sp1 and cAMP-response-element-binding protein-binding protein (CBP/p300)". Biochem. J. 339 (3): 751–8. doi:10.1042/0264-6021:3390751. PMC . PMID 10215616.
- Zhang H, Hu G, Wang H, Sciavolino P, Iler N, Shen MM, Abate-Shen C (May 1997). "Heterodimerization of Msx and Dlx homeoproteins results in functional antagonism". Mol. Cell. Biol. 17 (5): 2920–32. doi:10.1128/mcb.17.5.2920. PMC . PMID 9111364.
- Zhang H, Catron KM, Abate-Shen C (March 1996). "A role for the Msx-1 homeodomain in transcriptional regulation: residues in the N-terminal arm mediate TATA binding protein interaction and transcriptional repression". Proc. Natl. Acad. Sci. U.S.A. 93 (5): 1764–9. doi:10.1073/pnas.93.5.1764. PMC . PMID 8700832.
- 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 Res. 25 (11): 2174–81. doi:10.1093/nar/25.11.2174. PMC . PMID 9153318.
- Seto E, Usheva A, Zambetti GP, Momand J, Horikoshi N, Weinmann R, Levine AJ, Shenk T (December 1992). "Wild-type p53 binds to the TATA-binding protein and represses transcription". Proc. Natl. Acad. Sci. U.S.A. 89 (24): 12028–32. doi:10.1073/pnas.89.24.12028. PMC . PMID 1465435.
- Cvekl A, Kashanchi F, Brady JN, Piatigorsky J (June 1999). "Pax-6 interactions with TATA-box-binding protein and retinoblastoma protein". Invest. Ophthalmol. Vis. Sci. 40 (7): 1343–50. PMID 10359315.
- Zwilling S, Annweiler A, Wirth T (May 1994). "The POU domains of the Oct1 and Oct2 transcription factors mediate specific interaction with TBP". Nucleic Acids Res. 22 (9): 1655–62. doi:10.1093/nar/22.9.1655. PMC . PMID 8202368.
- Guermah M, Malik S, Roeder RG (June 1998). "Involvement of TFIID and USA components in transcriptional activation of the human immunodeficiency virus promoter by NF-kappaB and Sp1". Mol. Cell. Biol. 18 (6): 3234–44. doi:10.1128/mcb.18.6.3234. PMC . PMID 9584164.
- Schmitz ML, Stelzer G, Altmann H, Meisterernst M, Baeuerle PA (March 1995). "Interaction of the COOH-terminal transactivation domain of p65 NF-kappa B with TATA-binding protein, transcription factor IIB, and coactivators". J. Biol. Chem. 270 (13): 7219–26. doi:10.1074/jbc.270.13.7219. PMID 7706261.
- Schulman IG, Chakravarti D, Juguilon H, Romo A, Evans RM (August 1995). "Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation". Proc. Natl. Acad. Sci. U.S.A. 92 (18): 8288–92. doi:10.1073/pnas.92.18.8288. PMC . PMID 7667283.
- Siegert JL, Robbins PD (January 1999). "Rb inhibits the intrinsic kinase activity of TATA-binding protein-associated factor TAFII250". Mol. Cell. Biol. 19 (1): 846–54. PMC . PMID 9858607.
- Ruppert S, Wang EH, Tjian R (March 1993). "Cloning and expression of human TAFII250: a TBP-associated factor implicated in cell-cycle regulation". Nature. 362 (6416): 175–9. doi:10.1038/362175a0. PMID 7680771.
- O'Brien T, Tjian R (May 1998). "Functional analysis of the human TAFII250 N-terminal kinase domain". Mol. Cell. 1 (6): 905–11. doi:10.1016/S1097-2765(00)80089-1. PMID 9660973.
- 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". J. Cell. Sci. 116 (Pt 9): 1847–58. doi:10.1242/jcs.00391. PMID 12665565.
- Tao Y, Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder RG (March 1997). "Specific interactions and potential functions of human TAFII100". J. Biol. Chem. 272 (10): 6714–21. doi:10.1074/jbc.272.10.6714. PMID 9045704.
- Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (October 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 . PMID 11564863.
- Mengus G, May M, Jacq X, Staub A, Tora L, Chambon P, Davidson I (April 1995). "Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID". EMBO J. 14 (7): 1520–31. PMC . PMID 7729427.
- May M, Mengus G, Lavigne AC, Chambon P, Davidson I (June 1996). "Human TAF(II28) promotes transcriptional stimulation by activation function 2 of the retinoid X receptors". EMBO J. 15 (12): 3093–104. PMC . PMID 8670810.
- Hoffmann A, Roeder RG (July 1996). "Cloning and characterization of human TAF20/15. Multiple interactions suggest a central role in TFIID complex formation". J. Biol. Chem. 271 (30): 18194–202. doi:10.1074/jbc.271.30.18194. PMID 8663456.
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Transcription factor TFIID (or TATA-binding protein, TBP) Provide feedback
No Pfam abstract.
Hoffman A, Sinn E, Yamamoto T, Wang J, Roy A, Horikoshi M, Roeder RG; , Nature 1990;346:387-390.: Highly conserved core domain and unique N terminus with presumptive regulatory motifs in a human TATA factor (TFIID). PUBMED:2374612 EPMC:2374612
Internal database links
|SCOOP:||DUF3252 DUF3378 T4bSS_IcmS DUF4295|
|Similarity to PfamA using HHSearch:||DUF3378|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000814
The TATA-box binding protein (TBP) is required for the initiation of transcription by RNA polymerases I, II and III, from promoters with or without a TATA box [PUBMED:12782648, PUBMED:10974559]. TBP associates with a host of factors, including the general transcription factors TFIIA, -B, -D, -E, and -H, to form huge multi-subunit pre-initiation complexes on the core promoter. Through its association with different transcription factors, TBP can initiate transcription from different RNA polymerases. There are several related TBPs, including TBP-like (TBPL) proteins [PUBMED:12878007].
The C-terminal core of TBP (~180 residues) is highly conserved and contains two 77-amino acid repeats that produce a saddle-shaped structure that straddles the DNA; this region binds to the TATA box and interacts with transcription factors and regulatory proteins [PUBMED:1436073]. By contrast, the N-terminal region varies in both length and sequence.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||DNA binding (GO:0003677)|
|Biological process||DNA-templated transcription, initiation (GO:0006352)|
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TBP is a transcription factor whose DNA binding fold is composed of a curved antiparallel beta-sheet . This fold is also found in the N terminal region of DNA repair glycosylases. The N terminal domain of DNA glycosylase has only a single copy of the fold, whereas TBP contains a duplication of this fold [2-3].
The clan contains the following 4 members:AlkA_N DUF3378 OGG_N TBP
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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|Number in seed:||323|
|Number in full:||2735|
|Average length of the domain:||81.60 aa|
|Average identity of full alignment:||39 %|
|Average coverage of the sequence by the domain:||61.33 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 17690987 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||19|
|Download:||download the raw HMM for this family|
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The tree is built by considering the taxonomic lineage of each sequence that has a match to this family. For each node in the resulting tree, we draw an arc in the sunburst. The radius of the arc, its distance from the root node at the centre of the sunburst, shows the taxonomic level ("superkingdom", "kingdom", etc). The length of the arc represents either the number of sequences represented at a given level, or the number of species that are found beneath the node in the tree. The weighting scheme can be changed using the sunburst controls.
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There are some situations that the sunburst tree cannot easily handle and for which we have work-arounds in place.
Missing taxonomic levels
Some species in the taxonomic tree may not have one or more of the main eight levels that we display. For example, Bos taurus is not assigned an order in the NCBI taxonomic tree. In such cases we mark the omitted level with, for example, "No order", in both the tooltip and the lineage summary.
Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
So that these nodes are not simply omitted from the sunburst tree, we group them together in a separate branch (or segment of the sunburst tree). Since we cannot determine the lineage for these unmapped species, we show all levels between the superkingdom and the species as "uncategorised".
Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
Too many species/sequences
For large species trees, you may see blank regions in the outer layers of the sunburst. These occur when there are large numbers of arcs to be drawn in a small space. If an arc is less than approximately one pixel wide, it will not be drawn and the space will be left blank. You may still be able to get some information about the species in that region by moving your mouse across the area, but since each arc will be very small, it will be difficult to accurately locate a particular species.
The tree shows the occurrence of this domain across different species. More...
We show the species tree in one of two ways. For smaller trees we try to show an interactive representation, which allows you to select specific nodes in the tree and view them as an alignment or as a set of Pfam domain graphics.
Unfortunately we have found that there are problems viewing the interactive tree when the it becomes larger than a certain limit. Furthermore, we have found that Internet Explorer can become unresponsive when viewing some trees, regardless of their size. We therefore show a text representation of the species tree when the size is above a certain limit or if you are using Internet Explorer to view the site.
If you are using IE you can still load the interactive tree by clicking the "Generate interactive tree" button, but please be aware of the potential problems that the interactive species tree can cause.
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.
We also count the number of unique sequences on which each domain is found, which is shown in green. Note that a domain may appear multiple times on the same sequence, leading to the difference between these two numbers.
Finally, we group sequences from the same organism according to the NCBI code that is assigned by UniProt, allowing us to count the number of distinct sequences on which the domain is found. This value is shown in the pink boxes.
We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
You can use the tree controls to manipulate how the interactive tree is displayed:
- show/hide the summary boxes
- highlight species that are represented in the seed alignment
- expand/collapse the tree or expand it to a given depth
- select a sub-tree or a set of species within the tree and view them graphically or as an alignment
- save a plain text representation of the tree
Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.
There are 8 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 TBP domain has been found. There are 148 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.
Loading structure mapping...