関: TATA-box binding protein、TBP

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executed with proper legal authority; "a binding contract"
the protective covering on the front, back, and spine of a book; "the book had a leather binding" (同)book binding, cover, back
strip sewn over or along an edge for reinforcement or decoration
the capacity to attract and hold something
any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"

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義務的な,拘束力ある / 〈U〉しばること;〈C〉しばる物 / 〈C〉製本,装丁 / 〈U〉縁(‘ふち')取り材料
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/04/29 09:33:42」(JST)

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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.^[1] 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.^[2] 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.^[3]

Role as Transcription Factor Subunit

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 necessary component of RNA polymerase I and RNA polymerase III, and is, it is thought, the only common subunit required by all three of the RNA polymerases.

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. It is interesting to note that 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.

Interactions

TATA-binding protein has been shown to interact with:

BRF1,^[4]^[5]
BTAF1,^[6]^[7]
C-Fos,^[8]
C-jun,^[9]
EDF1,^[10]^[11]^[12]
GTF2B (TFIIB),^[13]^[14]
GTF2A1 (TFIIA subunit 1),^[13]^[15]^[16]^[17]
GTF2F1 (TFIIF subunit 1)^[6]^[18]^[19]
GTF2H4 (TFIIH subunit 4),^[6]
Mdm2,^[20]^[21]^[20]
MSX1,^[22]^[23]^[24]
NFYB,^[25]
P53,^[26]^[27]
PAX6,^[27]
POLR2A,^[6]
POU2F1,^[28]
RELA,^[29]^[30]
NR2B1,^[31]
TAF1,^[25]^[32]^[33]^[34]
TAF4,^[35]
TAF5,^[25]^[33]^[36]
TAF6,^[25]^[33]^[35]
TAF7,^[25]^[35]
TAF9.^[25]^[37]
TAF10,^[25]^[33]
TAF11,^[25]^[38]^[39]
TAF13,^[38] and
TAF15.^[40]

Complex Assembly

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.^[41]^[42] 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.^[43]

Structure

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 .^[44] By contrast, the N-terminal region varies in both length and sequence.

References

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^ Lee TI, Young RA (2000). "Transcription of eukaryotic protein-coding genes". Annu. Rev. Genet. 34: 77–137. doi:10.1146/annurev.genet.34.1.77. PMID 11092823.
^ "Entrez Gene: TBP TATA box binding protein".
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^ Wang Z, Roeder RG (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. doi:10.1073/pnas.92.15.7026. PMC 41464. PMID 7624363.
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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 42156. 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 19292. PMID 9482861.
^ ^a ^b 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 316412. 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 1220213. 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. PMC 232144. 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 39855. PMID 8700832.
^ ^a ^b ^c ^d ^e ^f ^g ^h 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 146709. 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 50691. PMID 1465435.
^ ^a ^b 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 308045. 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. PMC 108905. 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 41142. 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 83941. PMID 9858607.
^ ^a ^b ^c ^d 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.
^ ^a ^b ^c 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 99856. PMID 11564863.
^ ^a ^b 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 398239. 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 450252. 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.
^ Hochheimer A, Tjian R (June 2003). "Diversified transcription initiation complexes expand promoter selectivity and tissue-specific gene expression". Genes Dev. 17 (11): 1309–20. doi:10.1101/gad.1099903. PMID 12782648.
^ Pugh BF (September 2000). "Control of gene expression through regulation of the TATA-binding protein". Gene 255 (1): 1–14. PMID 10974559.
^ Davidson I (July 2003). "The genetics of TBP and TBP-related factors". Trends Biochem. Sci. 28 (7): 391–8. PMID 12878007.
^ Nikolov DB, Hu SH, Lin J, Gasch A, Hoffmann A, Horikoshi M, Chua NH, Roeder RG, Burley SK (November 1992). "Crystal structure of TFIID TATA-box binding protein". Nature 360 (6399): 40–6. doi:10.1038/360040a0. PMID 1436073.

External links

GeneReviews/NCBI/NIH/UW entry on Spinocerebellar Ataxia Type 17
Interactive TBP Structure at massey.ac.nz
PDB Molecule of the Month pdb67_1
TATA-Box Binding Protein at the US National Library of Medicine Medical Subject Headings (MeSH)
FactorBook TBP

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Basal transcription is regulated by lipopolysaccharide and glucosamine via the regulation of DNA binding of RNA polymerase II in RAW264.7 cells.

Hwang JS1, Hwang SY1, Han IO2.
Life sciences.Life Sci.2014 Aug 21;110(2):93-8. doi: 10.1016/j.lfs.2014.06.011. Epub 2014 Jun 23.
AIMS: The objective of this study is to investigate glucosamine (GlcN) as a transcriptional regulator of iNOS and other genes in association with the dynamic O-GlcNAcylation of RNA polymerase II (RNAPII).MAIN METHODS: The LPS- and/or GlcN-stimulated transcriptional activities of various Gal4-binding
PMID 24968300

The β-casein in camels: molecular characterization of the CSN2 gene, promoter analysis and genetic variability.

Pauciullo A1, Giambra IJ2, Iannuzzi L3, Erhardt G2.
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The β-casein is the most abundant protein in camel milk and its encoding gene (CSN2) is considered in other species a 'major' gene for the presence of alleles associated to different level of expression. In the present paper, we report for the first time the characterization of the nucleotide seque
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α-Phellandrene Alters Expression of Genes Associated with DNA Damage, Cell Cycle, and Apoptosis in Murine Leukemia WEHI-3 Cells.

Lin JJ1, Yu CC2, Lu KW3, Chang SJ2, Yu FS4, Liao CL3, Lin JG5, Chung JG6.
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α-phellandrene (α-PA) is a cyclic monoterpene, present in natural plants such as Schinus molle L. α-PA promotes immune responses in mice in vivo. However, there is no available information on whether α-PA affects gene expression in leukemia cells. The present study determined effects of α-PA on
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Japanese Journal

Perturbation of Discrete Sites on a Single Protein Domain with RNA Aptamers : Targeting of Different Sides of the TATA-Binding Protein (TBP)

HOHMURA Ken I,SHI Hua,HIRAYOSHI Kazunori
Bioscience, Biotechnology, and Biochemistry 77(8), 1739-1746, 2013-08
NAID 40019760145

Perturbation of Discrete Sites on a Single Protein Domain with RNA Aptamers: Targeting of Different Sides of the TATA-Binding Protein (TBP)

HOHMURA Ken I,SHI Hua,HIRAYOSHI Kazunori
Bioscience, Biotechnology, and Biochemistry, 2013
… Here we describe a novel selection procedure for RNA aptamers against a protein that constitutes a single structural domain, the Drosophila TATA-binding protein (TBP). … In addition to the conventional filter partitioning method with free TBP as target, we performed another experiment, in which the TATA-bound form of TBP was targeted. …
NAID 130003361198

A Small Trinucleotide Expansion in the TBP Gene Gives Rise to a Sporadic Case of SCA17 with Abnormal Putaminal Findings on MRI

Watanabe Mitsunori,Monai Natsuki,Jackson Mandy,Yamamoto-Watanabe Yukiko,Ikeda Yoshio,Suzuki Chieko,Tomiyama Masahiko,Kawarabayashi Takeshi,Kimura Tamaki,Seino Yusuke,Wakasaya Yasuhito,Miki Yasuo,Matsubara Etsuro,Shoji Mikio
Internal Medicine 47(24), 2179-2182, 2008
… We identified a heterozygously expanded CAG/CAA repeat (45/36) within the TATA-binding protein gene, leading to a diagnosis of SCA17. …
NAID 130000079782

Related Pictures

★リンクテーブル★

リンク元	「TATA結合タンパク質」「TBP」「TATA-box binding protein」
拡張検索	「TATA-binding protein associated factor」
関連記事	「binding」「TA」「binding protein」「TAT」

「TATA結合タンパク質」

TATA box binding protein
	; PDB rendering based on 1c9b.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1C9B, 1CDW, 1JFI, 1NVP, 1TGH
Identifiers
Symbols	TBP; GTF2D; GTF2D1; HDL4; SCA17; TFIID
External IDs	OMIM: 600075 MGI: 101838 HomoloGene: 2404 GeneCards: TBP Gene
Gene Ontology
Molecular function	• RNA polymerase II repressing transcription factor binding; • sequence-specific DNA binding transcription factor activity; • protein binding; • transcription factor binding; • transcription regulatory region DNA binding; • repressing transcription factor binding;
Cellular component	• female pronucleus; • male pronucleus; • nucleoplasm; • transcription factor TFIID complex; • transcription factor TFIIA complex; • nuclear euchromatin; • cytoplasm;
Biological process	• transcription from RNA polymerase II promoter; • transcription initiation from RNA polymerase II promoter; • transcription elongation from RNA polymerase II promoter; • transcription from RNA polymerase III promoter; • spermatogenesis; • cell death; • gene expression; • viral reproduction; • virus-host interaction; • positive regulation of transcription, DNA-dependent;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	This box: view; talk; edit;

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

TBP
	; crystal structure of a yeast brf1-tbp-dna ternary complex
Identifiers
Symbol	TBP
Pfam	PF00352
Pfam clan	CL0407
InterPro	IPR000814
PROSITE	PDOC00303
SCOP	1tbp
SUPERFAMILY	1tbp
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary