TATA-bindingsproteïne

Animatie van de dubbele-helixstructuur van een stuk DNA.^[2] De basenparen liggen horizontaal tussen de twee strengen in. De grote en de kleine groeve tussen de strengen zijn goed zichtbaar.

De TATA-bindingsproteïne (TBP) is een basale transcriptiefactor dat zich specifiek aan de TATA-box bindt. Deze DNA-sequentie zit ongeveer 30 basenparen stroomopwaarts van het startcodon.^[3] De proteïne bestaat uit 339 aminozuren en heeft een atomaire massa van 37.698 dalton. De kern van de C-terminus bestaat uit ongeveer 180 residuen met twee 88 aminozurenrepeats (tandem repeat) met een zadelvormige, secundaire structuur. Deze secundaire structuur bindt aan de TATA-box en heeft een wisselwerking met transcriptiefactoren en genregulerende proteïnen.^[4]

De TATA-bindingsproteïne is betrokken bij het uit elkaar gaan van de dubbele DNA-helix door het DNA 80° te buigen (de AT-rijke sequentie gaat doordat de adenine en de thymine met twee waterstofbruggen met elkaar verbonden zijn gemakkelijker uit elkaar, dan de andere nucleobasen die met drie waterstofbruggen met elkaar verbonden zijn). De TATA-bindingsproteïne is een ongebruikelijke proteïne daar het aan de kleine groeve van het DNA met een β-sheet bindt. Door de zijketens van de aminozuren van de TATA-bindingsproteïne tussen de basenparen te brengen ontwindt de dubbele helix gedeeltelijk en buigt deze twee keer. De buiging komt tot stand door een groot oppervlakcontact tussen de bindingsproteïne en het DNA. De TATA-bindingsproteïne bindt de negatief geladen fosfaten in het DNA aan de positief geladen lysine- en arginine-aminozuurresiduen. De buiging ontstaat uiteindelijk door vier omvangrijke phenylalanine-residuen in de kleine groef.

Promotor-DNA
|------------------------------------------|
Startpunt
stroomopwaarts ~17 basen doelwit-gen +1 stroomafwaarts
5'----------|-35|---------|-10|----------------------|A|------------3'
3'----------|-35|---------|-10|----------------------|T|------------5'

5'|A--------------------→3'
RNA

Het gedeelte bij -10 noemt men de TATA-box. De TATA-box wordt herkend en gebonden door de TATA-bindingsproteïne van het TFIID-complex (Transcriptie factor II D). Vervolgens koppelt het RNA-polymerase aan een DNA- of RNA-keten en vouwt zich eromheen, waarna de transcriptie of translatie vanaf het startcodon 10 basenparen verderop begint.

Een ander onderscheidend kenmerk van de TATA-bindingsproteïne is de lange streng van glutaminen in de N-terminus van de proteïne. Dit gebied reguleert de DNA-bindingsactiviteit van de C-terminus en dit beïnvloedt de mate waarin het transcriptiecomplex gevormd wordt en de initiatie van de transcriptie.^[5]

Mutaties die het aantal CAG-repeats coderen van dit polyglutamine gebied en dus de polyglutamine streng langer maken, zijn in verband gebracht met verschillende ziekten.

Polyglutamineziekten[bewerken | brontekst bewerken]

Bij de polyglutamineziekten bestaat het repetitieve codon uit de sequentie CAG en codeert bij de translatie voor het aminozuur glutamine.

Polyglutamineziekten^[6]
Type	Vererving	Gen	Repeateenheid	Repeatlocatie	Normale repeatlengte	Pathogene repeatlengte
Ziekte van Huntington (HD)	AD	Huntingtine (HDD)	(CAG)_n	N-Terminus	6–34	36–121
Dentatorubrale-pallidoluysiane atrofie (DRPLA)	AD	Atrofine	(CAG)_n	N-Terminus	7–34	49–88
Ziekte van Kennedy (SBMA)	XLR	Androgene receptor	(CAG)_n	N-Terminus	9–36	38–62
Spinocerebellaire ataxie Typ 1 (SCA1)	AD	Ataxine 1 (ATXN1)	(CAG)_n	N-Terminus	6–44	39–82
Spinocerebellaire ataxie Typ 2 (SCA2)	AD	Ataxine 2 (ATXN2)	(CAG)_n	N-Terminus	15–24	32–200
Spinocerebellaire ataxie Typ 3 (Machado-Joseph-ziekte, SCA3)	AD	Ataxine 3 (ATXN3)	(CAG)_n	C-Terminus	13–36	61–84
Spinocerebellaire ataxie Typ 6 (SCA6)	AD	CACNA1A	(CAG)_n	C-Terminus	4–19	10–33
Spinocerebellaire ataxie Typ 7 (SCA7)	AD	Ataxine 7 (ATXN7)	(CAG)_n	N-Terminus	4–35	37–306
Spinocerebellaire ataxie Typ 17 (SCA17)	AD	TBP	(CAG)_n		25–42	47–63

Rol als transcriptiefactor[bewerken | brontekst bewerken]

De TATA-bindingsproteïne is een onderdeel van de eukaryotische transcriptiefactor TFIID. TFIID is de eerste proteïne dat met het DNA een verbinding aangaat tijdens de vorming van het transcriptiecomplex van RNA-polymerase II (RNA Pol II), dat vooraf gaat aan de transcriptie. Met de binding van de TFIID aan de TATA-box in het promotorgebied van het gen start het inzetten van andere verbindingen, die voor RNA Pol II nodig zijn voor het beginnen van de transcriptie. Sommige van deze verbindingen zijn de transcriptiefactoren TFIIA, TFIIB en TFIIF. Deze transcriptiefactoren worden op hun beurt weer gevormd door de interactie van vele proteïne subeenheden. Transcriptie is dus een sterk gereguleerd proces.

De TATA-bindingsproteïne is ook een onderdeel van RNA-polymerase I en RNA-polymerase III en daardoor betrokken bij alle drie RNA-polymerasen.^[7] In specifieke celtypen of specifieke promotoren kan de TATA-bindingsproteïne vervangen zijn door een of verscheidene op aan TBP gerelateerde proteïnen.^[8]

Transcriptiefactoren[bewerken | brontekst bewerken]

Promotor element	Transcriptiefactor	Transcriptiefactor-functie	Consensus sequentie
BRE	TFIIB	Positionering van RNA-polymerase ten opzichte van de transcriptie start.	G/C G/C G/A C G C C
TATA	TBP	TATA-bindingsproteïne. Opbouw transcriptiecomplex, aantrekken van TFIIB, onderdeel van TFIID.	T A T A A/T A A/T
INR	TFIID	Herkenning TATA-box, opbouw transcriptiecomplex, aantrekken van TFIIB.	C/T C/T A n T/A C/T C/T
DPE	TFIID	Herkenning TATA-box, opbouw transcriptiecomplex, aantrekken van TFIIB.	A/G G A/T C G T G
	TFIIF	Stabiliseert interactie tussen TBP/TFIIB en RNA-polymerase, trekt TFIIE en TFIIH aan.
	TFIIE	Aantrekken en reguleren van TFIIH.
	TFIIH	Helicase-activiteit, laat RNA-polymerase los.

Proteïne–proteïne-interacties[bewerken | brontekst bewerken]

De TATA-bindingsproteïne heeft proteïne-proteïne-interacties met:

BRF1,^[9]^[10]
BTAF1,^[11]^[12]
C-Fos,^[13]
C-jun,^[14]
EDF1,^[15]^[16]^[17]
GTF2B (TFIIB),^[18]^[19]
GTF2A1 (TFIIA subunit 1),^[18]^[20]^[21]^[22]
GTF2F1 (TFIIF subunit 1)^[11]^[23]^[24]
GTF2H4 (TFIIH subunit 4),^[11]
Mdm2,^[25]^[25]^[26]
MSX1,^[27]^[28]^[29]
NFYB,^[30]
P53,^[31]^[32]
PAX6,^[32]
POLR2A,^[11]
POU2F1,^[33]
RELA,^[34]^[35]
NR2B1,^[36]
TAF1,^[30]^[37]^[38]^[39]
TAF4,^[40]
TAF5,^[30]^[38]^[41]
TAF6,^[30]^[38]^[40]
TAF7,^[30]^[40]
TAF9.^[30]^[42]
TAF10,^[30]^[38]
TAF11,^[30]^[43]^[44]
TAF13,^[43] and
TAF15.^[45]

Bronnen, noten en/of referenties

↑ Swint-Kruse L, Matthews KS (April 2009). Allostery in the LacI/GalR family: variations on a theme. Curr. Opin. Microbiol. 12 (2): 129–37. PMID 19269243. PMC 2688824. DOI: 10.1016/j.mib.2009.01.009.
↑ Gemaakt van PDB 1D65
↑ (2007). The molecular basis of eukaryotic transcription. Proc. Natl. Acad. Sci. U.S.A. 104 (32): 12955–61. PMID 17670940. PMC 1941834. DOI: 10.1073/pnas.0704138104.
↑ (November 1992). Crystal structure of TFIID TATA-box binding protein. Nature 360 (6399): 40–6. PMID 1436073. DOI: 10.1038/360040a0.
↑ Entrez Gene: TBP TATA box binding protein. Gearchiveerd op 7 maart 2010.
↑ H. T. Orr, H. Y. Zoghbi: Trinucleotide repeat disorders. In: Annual review of neuroscience. Band 30, 2007, S. 575–621, ISSN 0147-006X. DOI:10.1146/annurev.neuro.29.051605.113042. PMID 17417937. (Review).
↑ (February 2012). Conservation between the RNA polymerase I, II, and III transcription initiation machineries. Molecular Cell 45 (4): 439–46. PMID 22365827. DOI: 10.1016/j.molcel.2012.01.023.
↑ (1 January 2011). TBP-related factors: a paradigm of diversity in transcription initiation. Cell & Bioscience 1 (1): 23. PMID 21711503. PMC 3142196. DOI: 10.1186/2045-3701-1-23.
↑ (August 2000). Alternatively spliced hBRF variants function at different RNA polymerase III promoters. EMBO J. 19 (15): 4134–43. PMID 10921893. PMC 306597. DOI: 10.1093/emboj/19.15.4134.
↑ (July 1995). 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. Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7026–30. PMID 7624363. PMC 41464. DOI: 10.1073/pnas.92.15.7026.
↑ ^a ^b ^c ^d (May 1997). BRCA1 is a component of the RNA polymerase II holoenzyme. Proc. Natl. Acad. Sci. U.S.A. 94 (11): 5605–10. PMID 9159119. PMC 20825. DOI: 10.1073/pnas.94.11.5605.
↑ (March 1998). Cloning and biochemical characterization of TAF-172, a human homolog of yeast Mot1. Mol. Cell. Biol. 18 (3): 1701–10. PMID 9488487. PMC 108885.
↑ (September 1994). c-Fos-induced activation of a TATA-box-containing promoter involves direct contact with TATA-box-binding protein. Mol. Cell. Biol. 14 (9): 6021–9. PMID 8065335. PMC 359128. DOI: 10.1128/MCB.14.9.6021.
↑ (February 1995). In vitro association between the Jun protein family and the general transcription factors, TBP and TFIIB. Biochem. J. 305 (3): 967–74. PMID 7848298. PMC 1136352. DOI: 10.1042/bj3050967.
↑ (June 2002). Multiprotein bridging factor-1 (MBF-1) is a cofactor for nuclear receptors that regulate lipid metabolism. Mol. Endocrinol. 16 (6): 1367–77. PMID 12040021. DOI: 10.1210/mend.16.6.0843.
↑ (August 2000). Interaction between endothelial differentiation-related factor-1 and calmodulin in vitro and in vivo. J. Biol. Chem. 275 (31): 24047–51. PMID 10816571. DOI: 10.1074/jbc.M001928200.
↑ (November 1999). The role of human MBF1 as a transcriptional coactivator. J. Biol. Chem. 274 (48): 34196–202. PMID 10567391. DOI: 10.1074/jbc.274.48.34196.
↑ ^a ^b (February 1996). Protein–protein interactions in eukaryotic transcription initiation: structure of the preinitiation complex. Proc. Natl. Acad. Sci. U.S.A. 93 (3): 1119–24. PMID 8577725. PMC 40041. DOI: 10.1073/pnas.93.3.1119.
↑ (February 2004). Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms. Science 303 (5660): 983–8. PMID 14963322. DOI: 10.1126/science.1090838.
↑ (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. PMID 7724559. PMC 42156. DOI: 10.1073/pnas.92.8.3313.
↑ (June 1998). Transcription factor IIA derepresses TATA-binding protein (TBP)-associated factor inhibition of TBP-DNA binding. J. Biol. Chem. 273 (23): 14293–300. PMID 9603936. DOI: 10.1074/jbc.273.23.14293.
↑ (October 1994). Reconstitution of human TFIIA activity from recombinant polypeptides: a role in TFIID-mediated transcription. Genes Dev. 8 (19): 2336–48. PMID 7958900. DOI: 10.1101/gad.8.19.2336.
↑ (November 1995). Human TAFII250 interacts with RAP74: implications for RNA polymerase II initiation. Genes Dev. 9 (22): 2747–55. PMID 7590250. DOI: 10.1101/gad.9.22.2747.
↑ (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. PMID 9482861. PMC 19292. DOI: 10.1073/pnas.95.5.2192.
↑ ^a ^b (August 1997). Repression of p53-mediated transcription by MDM2: a dual mechanism. Genes Dev. 11 (15): 1974–86. PMID 9271120. PMC 316412. DOI: 10.1101/gad.11.15.1974.
↑ (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. PMID 9388200. DOI: 10.1074/jbc.272.49.30651.
↑ (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. PMID 10215616. PMC 1220213. DOI: 10.1042/0264-6021:3390751.
↑ (May 1997). Heterodimerization of Msx and Dlx homeoproteins results in functional antagonism. Mol. Cell. Biol. 17 (5): 2920–32. PMID 9111364. PMC 232144. DOI: 10.1128/mcb.17.5.2920.
↑ (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. PMID 8700832. PMC 39855. DOI: 10.1073/pnas.93.5.1764.
↑ ^a ^b ^c ^d ^e ^f ^g ^h (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. PMID 9153318. PMC 146709. DOI: 10.1093/nar/25.11.2174.
↑ (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. PMID 1465435. PMC 50691. DOI: 10.1073/pnas.89.24.12028.
↑ ^a ^b (June 1999). Pax-6 interactions with TATA-box-binding protein and retinoblastoma protein. Invest. Ophthalmol. Vis. Sci. 40 (7): 1343–50. PMID 10359315.
↑ (May 1994). The POU domains of the Oct1 and Oct2 transcription factors mediate specific interaction with TBP. Nucleic Acids Res. 22 (9): 1655–62. PMID 8202368. PMC 308045. DOI: 10.1093/nar/22.9.1655.
↑ (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. PMID 9584164. PMC 108905. DOI: 10.1128/mcb.18.6.3234.
↑ (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. PMID 7706261. DOI: 10.1074/jbc.270.13.7219.
↑ (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. PMID 7667283. PMC 41142. DOI: 10.1073/pnas.92.18.8288.
↑ (January 1999). Rb inhibits the intrinsic kinase activity of TATA-binding protein-associated factor TAFII250. Mol. Cell. Biol. 19 (1): 846–54. PMID 9858607. PMC 83941.
↑ ^a ^b ^c ^d (March 1993). Cloning and expression of human TAFII250: a TBP-associated factor implicated in cell-cycle regulation. Nature 362 (6416): 175–9. PMID 7680771. DOI: 10.1038/362175a0.
↑ (May 1998). Functional analysis of the human TAFII250 N-terminal kinase domain. Mol. Cell 1 (6): 905–11. PMID 9660973. DOI: 10.1016/S1097-2765(00)80089-1.
↑ ^a ^b ^c (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. PMID 12665565. DOI: 10.1242/jcs.00391.
↑ (March 1997). Specific interactions and potential functions of human TAFII100. J. Biol. Chem. 272 (10): 6714–21. PMID 9045704. DOI: 10.1074/jbc.272.10.6714.
↑ (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. PMID 11564863. PMC 99856. DOI: 10.1128/MCB.21.20.6782-6795.2001.
↑ ^a ^b (April 1995). Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID. EMBO J. 14 (7): 1520–31. PMID 7729427. PMC 398239.
↑ (June 1996). Human TAF(II28) promotes transcriptional stimulation by activation function 2 of the retinoid X receptors. EMBO J. 15 (12): 3093–104. PMID 8670810. PMC 450252.
↑ (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. PMID 8663456. DOI: 10.1074/jbc.271.30.18194.

[pmid19269243-1] Swint-Kruse L, Matthews KS (April 2009). Allostery in the LacI/GalR family: variations on a theme. Curr. Opin. Microbiol. 12 (2): 129–37. PMID 19269243. PMC 2688824. DOI: 10.1016/j.mib.2009.01.009.

[2] Gemaakt van PDB 1D65

[pmid17670940-3] (2007). The molecular basis of eukaryotic transcription. Proc. Natl. Acad. Sci. U.S.A. 104 (32): 12955–61. PMID 17670940. PMC 1941834. DOI: 10.1073/pnas.0704138104.

[pmid1436073-4] (November 1992). Crystal structure of TFIID TATA-box binding protein. Nature 360 (6399): 40–6. PMID 1436073. DOI: 10.1038/360040a0.

[5] Entrez Gene: TBP TATA box binding protein. Gearchiveerd op 7 maart 2010.

[Trinucleotide_repeat_disorders-6] H. T. Orr, H. Y. Zoghbi: Trinucleotide repeat disorders. In: Annual review of neuroscience. Band 30, 2007, S. 575–621, ISSN 0147-006X. DOI:10.1146/annurev.neuro.29.051605.113042. PMID 17417937. (Review).

[7] (February 2012). Conservation between the RNA polymerase I, II, and III transcription initiation machineries. Molecular Cell 45 (4): 439–46. PMID 22365827. DOI: 10.1016/j.molcel.2012.01.023.

[8] (1 January 2011). TBP-related factors: a paradigm of diversity in transcription initiation. Cell & Bioscience 1 (1): 23. PMID 21711503. PMC 3142196. DOI: 10.1186/2045-3701-1-23.

[pmid10921893-9] (August 2000). Alternatively spliced hBRF variants function at different RNA polymerase III promoters. EMBO J. 19 (15): 4134–43. PMID 10921893. PMC 306597. DOI: 10.1093/emboj/19.15.4134.

[pmid7624363-10] (July 1995). 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. Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7026–30. PMID 7624363. PMC 41464. DOI: 10.1073/pnas.92.15.7026.

[pmid9159119-11] (May 1997). BRCA1 is a component of the RNA polymerase II holoenzyme. Proc. Natl. Acad. Sci. U.S.A. 94 (11): 5605–10. PMID 9159119. PMC 20825. DOI: 10.1073/pnas.94.11.5605.

[pmid9488487-12] (March 1998). Cloning and biochemical characterization of TAF-172, a human homolog of yeast Mot1. Mol. Cell. Biol. 18 (3): 1701–10. PMID 9488487. PMC 108885.

[pmid8065335-13] (September 1994). c-Fos-induced activation of a TATA-box-containing promoter involves direct contact with TATA-box-binding protein. Mol. Cell. Biol. 14 (9): 6021–9. PMID 8065335. PMC 359128. DOI: 10.1128/MCB.14.9.6021.

[pmid7848298-14] (February 1995). In vitro association between the Jun protein family and the general transcription factors, TBP and TFIIB. Biochem. J. 305 (3): 967–74. PMID 7848298. PMC 1136352. DOI: 10.1042/bj3050967.

[pmid12040021-15] (June 2002). Multiprotein bridging factor-1 (MBF-1) is a cofactor for nuclear receptors that regulate lipid metabolism. Mol. Endocrinol. 16 (6): 1367–77. PMID 12040021. DOI: 10.1210/mend.16.6.0843.

[pmid10816571-16] (August 2000). Interaction between endothelial differentiation-related factor-1 and calmodulin in vitro and in vivo. J. Biol. Chem. 275 (31): 24047–51. PMID 10816571. DOI: 10.1074/jbc.M001928200.

[pmid10567391-17] (November 1999). The role of human MBF1 as a transcriptional coactivator. J. Biol. Chem. 274 (48): 34196–202. PMID 10567391. DOI: 10.1074/jbc.274.48.34196.

[Tang-18] (February 1996). Protein–protein interactions in eukaryotic transcription initiation: structure of the preinitiation complex. Proc. Natl. Acad. Sci. U.S.A. 93 (3): 1119–24. PMID 8577725. PMC 40041. DOI: 10.1073/pnas.93.3.1119.

[pmid14963322-19] (February 2004). Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms. Science 303 (5660): 983–8. PMID 14963322. DOI: 10.1126/science.1090838.

[pmid7724559-20] (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. PMID 7724559. PMC 42156. DOI: 10.1073/pnas.92.8.3313.

[pmid9603936-21] (June 1998). Transcription factor IIA derepresses TATA-binding protein (TBP)-associated factor inhibition of TBP-DNA binding. J. Biol. Chem. 273 (23): 14293–300. PMID 9603936. DOI: 10.1074/jbc.273.23.14293.

[pmid7958900-22] (October 1994). Reconstitution of human TFIIA activity from recombinant polypeptides: a role in TFIID-mediated transcription. Genes Dev. 8 (19): 2336–48. PMID 7958900. DOI: 10.1101/gad.8.19.2336.

[pmid7590250-23] (November 1995). Human TAFII250 interacts with RAP74: implications for RNA polymerase II initiation. Genes Dev. 9 (22): 2747–55. PMID 7590250. DOI: 10.1101/gad.9.22.2747.

[pmid9482861-24] (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. PMID 9482861. PMC 19292. DOI: 10.1073/pnas.95.5.2192.

[pmid9271120-25] (August 1997). Repression of p53-mediated transcription by MDM2: a dual mechanism. Genes Dev. 11 (15): 1974–86. PMID 9271120. PMC 316412. DOI: 10.1101/gad.11.15.1974.

[pmid9388200-26] (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. PMID 9388200. DOI: 10.1074/jbc.272.49.30651.

[pmid10215616-27] (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. PMID 10215616. PMC 1220213. DOI: 10.1042/0264-6021:3390751.

[pmid9111364-28] (May 1997). Heterodimerization of Msx and Dlx homeoproteins results in functional antagonism. Mol. Cell. Biol. 17 (5): 2920–32. PMID 9111364. PMC 232144. DOI: 10.1128/mcb.17.5.2920.

[pmid8700832-29] (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. PMID 8700832. PMC 39855. DOI: 10.1073/pnas.93.5.1764.

[pmid9153318-30] ↑ ^a ^b ^c ^d ^e ^f ^g ^h (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. PMID 9153318. PMC 146709. DOI: 10.1093/nar/25.11.2174.

[pmid1465435-31] (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. PMID 1465435. PMC 50691. DOI: 10.1073/pnas.89.24.12028.

[pmid10359315-32] (June 1999). Pax-6 interactions with TATA-box-binding protein and retinoblastoma protein. Invest. Ophthalmol. Vis. Sci. 40 (7): 1343–50. PMID 10359315.

[pmid8202368-33] (May 1994). The POU domains of the Oct1 and Oct2 transcription factors mediate specific interaction with TBP. Nucleic Acids Res. 22 (9): 1655–62. PMID 8202368. PMC 308045. DOI: 10.1093/nar/22.9.1655.

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