View source for TATA-binding protein

{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Use dmy dates|date=April 2016}}
{{Infobox_gene}}
{{Infobox protein family
| Symbol = TBP
| Name = TBP
| image = PDB 1ngm EBI.jpg
| width = 270px
| caption = crystal structure of a yeast brf1-tbp-dna ternary complex
| Pfam = PF00352
| Pfam_clan = CL0407 
| InterPro = IPR000814
| SMART = 
| PROSITE = PDOC00303
| MEROPS = 
| SCOP = 1tbp
| TCDB = 
| OPM family = 
| OPM protein = 
| CAZy = 
| CDD = 
}}
The '''TATA-binding protein''' ('''TBP''') is a [[general transcription factor]] that binds to a [[DNA]] sequence called the [[TATA box]].  This DNA sequence is found about 30 [[base pair]]s upstream of the [[transcription start site]] in some [[eukaryote|eukaryotic]] [[gene]] [[promotor (biology)|promoter]]s.<ref name="pmid17670940">{{cite journal | vauthors = Kornberg RD | title = The molecular basis of eukaryotic transcription | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 104 | issue = 32 | pages = 12955–61 | year = 2007 | pmid = 17670940 | pmc = 1941834 | doi = 10.1073/pnas.0704138104 | bibcode = 2007PNAS..10412955K | doi-access = free }}</ref>

== TBP gene family ==

TBP is a member of a small gene family of TBP-related factors.<ref>{{cite journal | vauthors = Akhtar W, Veenstra GJ | title = TBP-related factors: a paradigm of diversity in transcription initiation | journal = Cell & Bioscience | volume = 1 | issue = 1 | pages = 23 | date = 1 January 2011 | pmid = 21711503 | pmc = 3142196 | doi = 10.1186/2045-3701-1-23 | doi-access = free }}</ref> The first TBP-related factor (TRF/TRF1) was identified in the fruit fly [[Drosophila]], but appears to be fly or insect-specific. Subsequently [[TBPL1]]/TRF2 was found in the genomes of many [[metazoa]]ns, whereas [[vertebrate]] genomes encode a third vertebrate family member, [[Tata-box binding protein like 2|TBPL2]]/TRF3. In specific cell types or on specific promoters TBP can be replaced by one of these TBP-related factors, some of which interact with the TATA box similarly to TBP.

== Role as transcription factor ==

TBP is a subunit of the eukaryotic [[general transcription factor]] [[TFIID]]. TFIID is the first protein to bind to DNA during the formation of the [[transcription preinitiation complex]] of [[RNA polymerase II]] (RNA Pol II).<ref name="pmid11092823">{{cite journal | vauthors = Lee TI, Young RA | title = Transcription of eukaryotic protein-coding genes | journal = Annual Review of Genetics | volume = 34 | pages = 77–137 | year = 2000 | pmid = 11092823 | doi = 10.1146/annurev.genet.34.1.77 }}</ref> 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 - the majority of human promoters are [[TATA box|TATA]]-less [[housekeeping gene]] [[Promoter (genetics)|promoters]] - so TBP is probably not the only protein involved in positioning RNA polymerase II.. The binding of TBP to these promoters is facilitated by housekeeping gene regulators.<ref>{{cite journal | vauthors = Lam KC, Mühlpfordt F, Vaquerizas JM, Raja SJ, Holz H, Luscombe NM, Manke T, Akhtar A | title = The NSL complex regulates housekeeping genes in Drosophila | journal = PLOS Genetics | volume = 8 | issue = 6 | pages = e1002736 | date = 2012 | pmid = 22723752 | pmc = 3375229 | doi = 10.1371/journal.pgen.1002736 | doi-access = free }}</ref><ref name=":0">{{cite journal | vauthors = Lam KC, Chung HR, Semplicio G, Iyer SS, Gaub A, Bhardwaj V, Holz H, Georgiev P, Akhtar A | title = The NSL complex-mediated nucleosome landscape is required to maintain transcription fidelity and suppression of transcription noise | journal = Genes & Development | volume = 33 | issue = 7–8 | pages = 452–465 | date = February 2019 | pmid = 30819819 | pmc = 6446542 | doi = 10.1101/gad.321489.118 }}</ref> Interestingly, transcription initiates within a narrow region at around 30 bp downstream of TATA box on TATA-containing promoters,<ref>{{cite journal | vauthors = Carninci P, Sandelin A, Lenhard B, Katayama S, Shimokawa K, Ponjavic J, Semple CA, Taylor MS, Engström PG, Frith MC, Forrest AR, Alkema WB, Tan SL, Plessy C, Kodzius R, Ravasi T, Kasukawa T, Fukuda S, Kanamori-Katayama M, Kitazume Y, Kawaji H, Kai C, Nakamura M, Konno H, Nakano K, Mottagui-Tabar S, Arner P, Chesi A, Gustincich S, Persichetti F, Suzuki H, Grimmond SM, Wells CA, Orlando V, Wahlestedt C, Liu ET, Harbers M, Kawai J, Bajic VB, Hume DA, Hayashizaki Y | display-authors = 6 | title = Genome-wide analysis of mammalian promoter architecture and evolution | journal = Nature Genetics | volume = 38 | issue = 6 | pages = 626–35 | date = June 2006 | pmid = 16645617 | doi = 10.1038/ng1789 | s2cid = 22205897 }}</ref> while transcription start sites of TATA-less promoters are dispersed within a 200 bp region.<ref>{{cite journal | vauthors = Ni T, Corcoran DL, Rach EA, Song S, Spana EP, Gao Y, Ohler U, Zhu J | title = A paired-end sequencing strategy to map the complex landscape of transcription initiation | journal = Nature Methods | volume = 7 | issue = 7 | pages = 521–7 | date = July 2010 | pmid = 20495556 | pmc = 3197272 | doi = 10.1038/nmeth.1464 }}</ref><ref name=":0" />

Binding of TFIID to the [[TATA box]] in the [[promotor (biology)|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 contains several protein subunits.

TBP is also important for transcription by [[RNA polymerase I]] and [[RNA polymerase III]], and is therefore involved in transcription initiation by all three RNA polymerases.<ref>{{cite journal | vauthors = Vannini A, Cramer P | title = Conservation between the RNA polymerase I, II, and III transcription initiation machineries | journal = Molecular Cell | volume = 45 | issue = 4 | pages = 439–46 | date = February 2012 | pmid = 22365827 | doi = 10.1016/j.molcel.2012.01.023 | doi-access = free | hdl = 11858/00-001M-0000-0015-483A-5 | hdl-access = free }}</ref>

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]].<ref>{{cite web | title = Entrez Gene: TBP TATA box binding protein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6908}}</ref>

== DNA-protein interactions ==

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. This incompleteness allows DNA to be passively bent on binding.

For information on the use of TBP in cells see: [[RNA polymerase I]], [[RNA polymerase II]], and [[RNA polymerase III]].

== Protein–protein interactions ==
TATA-binding protein has been shown to [[Protein–protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[BRF1 (gene)|BRF1]],<ref name="pmid10921893">{{cite journal | vauthors = McCulloch V, Hardin P, Peng W, Ruppert JM, Lobo-Ruppert SM | title = Alternatively spliced hBRF variants function at different RNA polymerase III promoters | journal = EMBO J. | volume = 19 | issue = 15 | pages = 4134–43  | date = August 2000 | pmid = 10921893 | pmc = 306597 | doi = 10.1093/emboj/19.15.4134 }}</ref><ref name="pmid7624363">{{cite journal | vauthors = Wang Z, Roeder RG | title = Structure and function of a human transcription factor TFIIIB subunit that is evolutionarily conserved and contains both TFIIB- and high-mobility-group protein 2-related domains | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 15 | pages = 7026–30  | date = July 1995 | pmid = 7624363 | pmc = 41464 | doi = 10.1073/pnas.92.15.7026 | bibcode = 1995PNAS...92.7026W | doi-access = free }}</ref>
* [[BTAF1]],<ref name=pmid9159119/><ref name="pmid9488487">{{cite journal | vauthors = Chicca JJ, Auble DT, Pugh BF | title = Cloning and biochemical characterization of TAF-172, a human homolog of yeast Mot1 | journal = Mol. Cell. Biol. | volume = 18 | issue = 3 | pages = 1701–10  | date = March 1998 | pmid = 9488487 | pmc = 108885 | doi =  10.1128/MCB.18.3.1701}}</ref>
* [[C-Fos]],<ref name="pmid8065335">{{cite journal | vauthors = Metz R, Bannister AJ, Sutherland JA, Hagemeier C, O'Rourke EC, Cook A, Bravo R, Kouzarides T | title = c-Fos-induced activation of a TATA-box-containing promoter involves direct contact with TATA-box-binding protein | journal = Mol. Cell. Biol. | volume = 14 | issue = 9 | pages = 6021–9  | date = September 1994 | pmid = 8065335 | pmc = 359128 | doi = 10.1128/MCB.14.9.6021 }}</ref>
* [[C-jun]],<ref name="pmid7848298">{{cite journal | vauthors = Franklin CC, McCulloch AV, Kraft AS | title = In vitro association between the Jun protein family and the general transcription factors, TBP and TFIIB | journal = Biochem. J. | volume = 305 | issue = 3 | pages = 967–74  | date = February 1995 | pmid = 7848298 | pmc = 1136352 | doi =  10.1042/bj3050967}}</ref>
* [[EDF1]],<ref name="pmid12040021">{{cite journal | vauthors = Brendel C, Gelman L, Auwerx J | title = Multiprotein bridging factor-1 (MBF-1) is a cofactor for nuclear receptors that regulate lipid metabolism | journal = Mol. Endocrinol. | volume = 16 | issue = 6 | pages = 1367–77  | date = June 2002 | pmid = 12040021 | doi = 10.1210/mend.16.6.0843 | doi-access = free }}</ref><ref name="pmid10816571">{{cite journal | vauthors = Mariotti M, De Benedictis L, Avon E, Maier JA | title = Interaction between endothelial differentiation-related factor-1 and calmodulin in vitro and in vivo | journal = J. Biol. Chem. | volume = 275 | issue = 31 | pages = 24047–51  | date = August 2000 | pmid = 10816571 | doi = 10.1074/jbc.M001928200 | doi-access = free }}</ref><ref name="pmid10567391">{{cite journal | vauthors = Kabe Y, Goto M, Shima D, Imai T, Wada T, ((Morohashi Ki)), Shirakawa M, Hirose S, Handa H | title = The role of human MBF1 as a transcriptional coactivator | journal = J. Biol. Chem. | volume = 274 | issue = 48 | pages = 34196–202  | date = November 1999 | pmid = 10567391 | doi = 10.1074/jbc.274.48.34196 | doi-access = free }}</ref>
* [[GTF2B]] (TFIIB),<ref name="Tang">{{cite journal |vauthors=Tang H, Sun X, Reinberg D, [[Richard H. Ebright|Ebright RH]] | title = Protein–protein interactions in eukaryotic transcription initiation: structure of the preinitiation complex | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 93 | issue = 3 | pages = 1119–24  | date = February 1996 | pmid = 8577725 | pmc = 40041 | doi = 10.1073/pnas.93.3.1119 | bibcode = 1996PNAS...93.1119T | doi-access = free }}</ref><ref name="pmid14963322">{{cite journal | vauthors = Bushnell DA, Westover KD, Davis RE, Kornberg RD | title = Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms | journal = Science | volume = 303 | issue = 5660 | pages = 983–8  | date = February 2004 | pmid = 14963322 | doi = 10.1126/science.1090838 | bibcode = 2004Sci...303..983B | s2cid = 36598301 }}</ref>
* [[GTF2A1]] ([[TFIIA]] subunit 1),<ref name=Tang /><ref name="pmid7724559">{{cite journal | vauthors = DeJong J, Bernstein R, Roeder RG | title = Human general transcription factor TFIIA: characterization of a cDNA encoding the small subunit and requirement for basal and activated transcription | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 8 | pages = 3313–7  | date = April 1995 | pmid = 7724559 | pmc = 42156 | doi = 10.1073/pnas.92.8.3313 | bibcode = 1995PNAS...92.3313D | doi-access = free }}</ref><ref name="pmid9603936">{{cite journal | vauthors = Ozer J, Mitsouras K, Zerby D, Carey M, Lieberman PM | title = Transcription factor IIA derepresses TATA-binding protein (TBP)-associated factor inhibition of TBP-DNA binding | journal = J. Biol. Chem. | volume = 273 | issue = 23 | pages = 14293–300  | date = June 1998 | pmid = 9603936 | doi = 10.1074/jbc.273.23.14293 | doi-access = free }}</ref><ref name="pmid7958900">{{cite journal | vauthors = Sun X, Ma D, Sheldon M, Yeung K, Reinberg D | title = Reconstitution of human TFIIA activity from recombinant polypeptides: a role in TFIID-mediated transcription | journal = Genes Dev. | volume = 8 | issue = 19 | pages = 2336–48  | date = October 1994 | pmid = 7958900 | doi = 10.1101/gad.8.19.2336 | doi-access = free }}</ref>
* [[GTF2F1]] ([[TFIIF]] subunit 1)<ref name=pmid9159119/><ref name="pmid7590250">{{cite journal | vauthors = Ruppert S, Tjian R | title = Human TAFII250 interacts with RAP74: implications for RNA polymerase II initiation | journal = Genes Dev. | volume = 9 | issue = 22 | pages = 2747–55  | date = November 1995 | pmid = 7590250 | doi = 10.1101/gad.9.22.2747 | doi-access = free }}</ref><ref name="pmid9482861">{{cite journal | vauthors = Malik S, Guermah M, Roeder RG | title = A dynamic model for PC4 coactivator function in RNA polymerase II transcription | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 95 | issue = 5 | pages = 2192–7  | date = March 1998 | pmid = 9482861 | pmc = 19292 | doi = 10.1073/pnas.95.5.2192 | bibcode = 1998PNAS...95.2192M | doi-access = free }}</ref>
* [[GTF2H4]] ([[TFIIH]] subunit 4),<ref name="pmid9159119">{{cite journal | vauthors = Scully R, Anderson SF, Chao DM, Wei W, Ye L, Young RA, Livingston DM, Parvin JD | title = BRCA1 is a component of the RNA polymerase II holoenzyme | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 94 | issue = 11 | pages = 5605–10  | date = May 1997 | pmid = 9159119 | pmc = 20825 | doi = 10.1073/pnas.94.11.5605 | bibcode = 1997PNAS...94.5605S | doi-access = free }}</ref>
* [[Mdm2]],<ref name="pmid9271120">{{cite journal | vauthors = Thut CJ, Goodrich JA, Tjian R | title = Repression of p53-mediated transcription by MDM2: a dual mechanism | journal = Genes Dev. | volume = 11 | issue = 15 | pages = 1974–86  | date = August 1997 | pmid = 9271120 | pmc = 316412 | doi = 10.1101/gad.11.15.1974 }}</ref><ref name="pmid9388200">{{cite journal | vauthors = Léveillard T, Wasylyk B | title = The MDM2 C-terminal region binds to TAFII250 and is required for MDM2 regulation of the cyclin A promoter | journal = J. Biol. Chem. | volume = 272 | issue = 49 | pages = 30651–61  | date = December 1997 | pmid = 9388200 | doi = 10.1074/jbc.272.49.30651 | doi-access = free }}</ref>
* [[MSX1]],<ref name="pmid10215616">{{cite journal | vauthors = Shetty S, Takahashi T, Matsui H, Ayengar R, Raghow R | title = 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) | journal = Biochem. J. | volume = 339 | issue = 3 | pages = 751–8  | date = May 1999 | pmid = 10215616 | pmc = 1220213 | doi = 10.1042/0264-6021:3390751 }}</ref><ref name="pmid9111364">{{cite journal | vauthors = Zhang H, Hu G, Wang H, Sciavolino P, Iler N, Shen MM, Abate-Shen C | title = Heterodimerization of Msx and Dlx homeoproteins results in functional antagonism | journal = Mol. Cell. Biol. | volume = 17 | issue = 5 | pages = 2920–32  | date = May 1997 | pmid = 9111364 | pmc = 232144 | doi =  10.1128/mcb.17.5.2920}}</ref><ref name="pmid8700832">{{cite journal | vauthors = Zhang H, Catron KM, Abate-Shen C | title = A role for the Msx-1 homeodomain in transcriptional regulation: residues in the N-terminal arm mediate TATA binding protein interaction and transcriptional repression | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 93 | issue = 5 | pages = 1764–9  | date = March 1996 | pmid = 8700832 | pmc = 39855 | doi = 10.1073/pnas.93.5.1764 | bibcode = 1996PNAS...93.1764Z | doi-access = free }}</ref>
* [[NFYB]],<ref name="pmid9153318">{{cite journal | vauthors = Bellorini M, Lee DK, Dantonel JC, Zemzoumi K, Roeder RG, Tora L, Mantovani R | title = 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 | journal = Nucleic Acids Res. | volume = 25 | issue = 11 | pages = 2174–81  | date = June 1997 | pmid = 9153318 | pmc = 146709 | doi = 10.1093/nar/25.11.2174 }}</ref>
* [[P53]],<ref name="pmid1465435">{{cite journal | vauthors = Seto E, Usheva A, Zambetti GP, Momand J, Horikoshi N, Weinmann R, Levine AJ, Shenk T | title = Wild-type p53 binds to the TATA-binding protein and represses transcription | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 89 | issue = 24 | pages = 12028–32  | date = December 1992 | pmid = 1465435 | pmc = 50691 | doi = 10.1073/pnas.89.24.12028 | bibcode = 1992PNAS...8912028S | doi-access = free }}</ref><ref name=pmid10359315/>
* [[PAX6]],<ref name="pmid10359315">{{cite journal | vauthors = Cvekl A, Kashanchi F, Brady JN, Piatigorsky J | title = Pax-6 interactions with TATA-box-binding protein and retinoblastoma protein | journal = Invest. Ophthalmol. Vis. Sci. | volume = 40 | issue = 7 | pages = 1343–50  | date = June 1999 | pmid = 10359315 }}</ref>
* [[POLR2A]],<ref name=pmid9159119/>
* [[POU2F1]],<ref name="pmid8202368">{{cite journal | vauthors = Zwilling S, Annweiler A, Wirth T | title = The POU domains of the Oct1 and Oct2 transcription factors mediate specific interaction with TBP | journal = Nucleic Acids Res. | volume = 22 | issue = 9 | pages = 1655–62  | date = May 1994 | pmid = 8202368 | pmc = 308045 | doi = 10.1093/nar/22.9.1655 }}</ref>
* [[RELA]],<ref name="pmid9584164">{{cite journal | vauthors = Guermah M, Malik S, Roeder RG | title = Involvement of TFIID and USA components in transcriptional activation of the human immunodeficiency virus promoter by NF-kappaB and Sp1 | journal = Mol. Cell. Biol. | volume = 18 | issue = 6 | pages = 3234–44  | date = June 1998 | pmid = 9584164 | pmc = 108905 | doi =  10.1128/mcb.18.6.3234}}</ref><ref name="pmid7706261">{{cite journal | vauthors = Schmitz ML, Stelzer G, Altmann H, Meisterernst M, Baeuerle PA | title = Interaction of the COOH-terminal transactivation domain of p65 NF-kappa B with TATA-binding protein, transcription factor IIB, and coactivators | journal = J. Biol. Chem. | volume = 270 | issue = 13 | pages = 7219–26  | date = March 1995 | pmid = 7706261 | doi = 10.1074/jbc.270.13.7219 | doi-access = free }}</ref>
* [[Retinoid X receptor alpha|NR2B1]],<ref name="pmid7667283">{{cite journal | vauthors = Schulman IG, Chakravarti D, Juguilon H, Romo A, Evans RM | title = Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 18 | pages = 8288–92  | date = August 1995 | pmid = 7667283 | pmc = 41142 | doi = 10.1073/pnas.92.18.8288 | bibcode = 1995PNAS...92.8288S | doi-access = free }}</ref>
* [[TAF1]],<ref name=pmid9153318/><ref name="pmid9858607">{{cite journal | vauthors = Siegert JL, Robbins PD | title = Rb inhibits the intrinsic kinase activity of TATA-binding protein-associated factor TAFII250 | journal = Mol. Cell. Biol. | volume = 19 | issue = 1 | pages = 846–54  | date = January 1999 | pmid = 9858607 | pmc = 83941 | doi =  10.1128/MCB.19.1.846}}</ref><ref name="pmid7680771">{{cite journal | vauthors = Ruppert S, Wang EH, Tjian R | title = Cloning and expression of human TAFII250: a TBP-associated factor implicated in cell-cycle regulation | journal = Nature | volume = 362 | issue = 6416 | pages = 175–9  | date = March 1993 | pmid = 7680771 | doi = 10.1038/362175a0 | bibcode = 1993Natur.362..175R | s2cid = 4364676 | doi-access = free }}</ref><ref name="pmid9660973">{{cite journal | vauthors = O'Brien T, Tjian R | title = Functional analysis of the human TAFII250 N-terminal kinase domain | journal = Mol. Cell | volume = 1 | issue = 6 | pages = 905–11  | date = May 1998 | pmid = 9660973 | doi = 10.1016/S1097-2765(00)80089-1 | doi-access = free }}</ref>
* [[TAF4]],<ref name="pmid12665565">{{cite journal | vauthors = Pointud JC, Mengus G, Brancorsini S, Monaco L, Parvinen M, Sassone-Corsi P, Davidson I | title = The intracellular localisation of TAF7L, a paralogue of transcription factor TFIID subunit TAF7, is developmentally regulated during male germ-cell differentiation | journal = J. Cell Sci. | volume = 116 | issue = Pt 9 | pages = 1847–58  | date = May 2003 | pmid = 12665565 | doi = 10.1242/jcs.00391 | s2cid = 24519687 | doi-access =  }}</ref>
* [[TAF5]],<ref name=pmid9153318/><ref name=pmid7680771/><ref name="pmid9045704">{{cite journal | vauthors = Tao Y, Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder RG | title = Specific interactions and potential functions of human TAFII100 | journal = J. Biol. Chem. | volume = 272 | issue = 10 | pages = 6714–21  | date = March 1997 | pmid = 9045704 | doi = 10.1074/jbc.272.10.6714 | doi-access = free }}</ref>
* [[TAF6]],<ref name=pmid9153318/><ref name=pmid7680771/><ref name=pmid12665565/>
* [[TAF7]],<ref name=pmid9153318/><ref name=pmid12665565/>
* [[TAF9]].<ref name=pmid9153318/><ref name="pmid11564863">{{cite journal | vauthors = Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG | title = Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo | journal = Mol. Cell. Biol. | volume = 21 | issue = 20 | pages = 6782–95  | date = October 2001 | pmid = 11564863 | pmc = 99856 | doi = 10.1128/MCB.21.20.6782-6795.2001 }}</ref>
* [[TAF10]],<ref name=pmid9153318/><ref name=pmid7680771/>
* [[TAF11]],<ref name=pmid9153318/><ref name=pmid7729427/><ref name="pmid8670810">{{cite journal | vauthors = May M, Mengus G, Lavigne AC, Chambon P, Davidson I | title = Human TAF(II28) promotes transcriptional stimulation by activation function 2 of the retinoid X receptors | journal = EMBO J. | volume = 15 | issue = 12 | pages = 3093–104  | date = June 1996 | pmid = 8670810 | pmc = 450252 | doi =  10.1002/j.1460-2075.1996.tb00672.x}}</ref>
* [[TAF13]],<ref name="pmid7729427">{{cite journal | vauthors = Mengus G, May M, Jacq X, Staub A, Tora L, Chambon P, Davidson I | title = Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID | journal = EMBO J. | volume = 14 | issue = 7 | pages = 1520–31  | date = April 1995 | pmid = 7729427 | pmc = 398239 | doi =  10.1002/j.1460-2075.1995.tb07138.x}}</ref> and
* [[TAF15]].<ref name="pmid8663456">{{cite journal | vauthors = Hoffmann A, Roeder RG | title = Cloning and characterization of human TAF20/15. Multiple interactions suggest a central role in TFIID complex formation | journal = J. Biol. Chem. | volume = 271 | issue = 30 | pages = 18194–202  | date = July 1996 | pmid = 8663456 | doi = 10.1074/jbc.271.30.18194 | doi-access = free }}</ref>
{{Div col end}}

==Complex assembly==
The TATA-box [[Binding (molecular)|binding]] [[protein]] (TBP) is required for the initiation of [[Transcription (genetics)|transcription]] by RNA [[polymerases]] I, II and III, from [[promotor (biology)|promoter]]s with or without a TATA box.<ref name="pmid12782648">{{cite journal | vauthors = Hochheimer A, Tjian R | title = Diversified transcription initiation complexes expand promoter selectivity and tissue-specific gene expression | journal = Genes & Development | volume = 17 | issue = 11 | pages = 1309–20 | date = June 2003 | pmid = 12782648 | doi = 10.1101/gad.1099903 | doi-access = free }}</ref><ref name="pmid10974559">{{cite journal | vauthors = Pugh BF | title = Control of gene expression through regulation of the TATA-binding protein | journal = Gene | volume = 255 | issue = 1 | pages = 1–14 | date = September 2000 | pmid = 10974559 | doi = 10.1016/s0378-1119(00)00288-2 }}</ref> In the presence of a TATA-less promoter, TBP binds with the help of TBP-associated factors (TAFs).<ref>{{Cite book|title=Molecular biology|author=Weaver, Robert Franklin|date=2012-01-01|publisher=McGraw-Hill|isbn=9780073525327|oclc=789601172}}</ref><ref>{{cite journal | vauthors = Louder RK, He Y, López-Blanco JR, Fang J, Chacón P, Nogales E | title = Structure of promoter-bound TFIID and model of human pre-initiation complex assembly | journal = Nature | volume = 531 | issue = 7596 | pages = 604–9 | date = March 2016 | pmid = 27007846 | pmc = 4856295 | doi = 10.1038/nature17394 | bibcode = 2016Natur.531..604L }}</ref> TBP associates with a host of factors, including the general [[transcription factor]]s TFIIA, -B, -D, -E, and -H, to form huge multi-subunit pre-initiation complexes on the core [[promoter (biology)|promoter]]. Through its association with different [[transcription (biology)|transcription]] factors, TBP can initiate [[transcription (genetics)|transcription]] from different RNA [[polymerase]]s. There are several related TBPs, including TBP-like (TBPL) [[protein]]s.<ref name="pmid12878007">{{cite journal | vauthors = Davidson I | title = The genetics of TBP and TBP-related factors | journal = Trends in Biochemical Sciences | volume = 28 | issue = 7 | pages = 391–8 | date = July 2003 | pmid = 12878007 | doi = 10.1016/S0968-0004(03)00117-8 }}</ref>

==Structure==
The C-terminal core of TBP (~180 residues) is [[Conservation (genetics)|highly conserved]] and contains two 88-amino acid [[tandem repeat|repeat]]s that produce a saddle-shaped [[secondary structure|structure]] that straddles the DNA; this region [[Molecular binding|bind]]s to the TATA box and [[Protein–protein interaction|interact]]s with [[transcription factor]]s and [[gene regulation|regulatory]] [[proteins]] .<ref name="pmid1436073">{{cite journal | vauthors = Nikolov DB, Hu SH, Lin J, Gasch A, Hoffmann A, Horikoshi M, Chua NH, Roeder RG, Burley SK | title = Crystal structure of TFIID TATA-box binding protein | journal = Nature | volume = 360 | issue = 6399 | pages = 40–6  | date = November 1992 | pmid = 1436073 | doi = 10.1038/360040a0 | bibcode = 1992Natur.360...40N | s2cid = 4307043 }}</ref> By contrast, the N-terminal region varies in both length and [[sequence (biology)|sequence]].

== References ==
{{Reflist|32em}}

== External links ==
* [https://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=gene&part=sca17 GeneReviews/NCBI/NIH/UW entry on Spinocerebellar Ataxia Type 17]
*[https://web.archive.org/web/20050907105851/http://www.massey.ac.nz/~wwbioch/DNAprot/DNAmelt/framset.htm Interactive TBP Structure at massey.ac.nz]
* {{PDB Molecule of the Month|67|TATA-binding protein}}
* {{MeshName|TATA-Box+Binding+Protein}}
* {{FactorBook|TBP}}
* {{PDBe-KB2|P20226|Human TATA-box-binding protein}}

{{PDB Gallery|geneid=6908}}
{{Transcription factors|g4}}

{{DEFAULTSORT:Tata-Binding Protein}}
[[Category:Proteins]]
[[Category:Genes]]
[[Category:Transcription factors]]