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TATA-vezujući protein

Nepregledano
S Wikipedije, slobodne enciklopedije
TATA-vezujući protein
Dostupne strukture
PDBPretraga ortologa: PDBe RCSB
Spisak PDB ID kodova

1TGH, 1C9B, 1JFI, 1NVP, 4ROC, 4ROE, 4ROD, 5IY9, 5IYA, 5FUR, 5IYC, 5IYB, 5IY7, 5IY8, 5IYD, 5IY6

Identifikatori
AliasiTBP
Vanjski ID-jeviOMIM: 600075 MGI: 101838 HomoloGene: 2404 GeneCards: TBP
Lokacija gena (čovjek)
Hromosom 6 (čovjek)
Hrom.Hromosom 6 (čovjek)[1]
Hromosom 6 (čovjek)
Genomska lokacija za TATA-vezujući protein
Genomska lokacija za TATA-vezujući protein
Bend6q27Početak170,554,302 bp[1]
Kraj170,572,870 bp[1]
Lokacija gena (miš)
Hromosom 17 (miš)
Hrom.Hromosom 17 (miš)[2]
Hromosom 17 (miš)
Genomska lokacija za TATA-vezujući protein
Genomska lokacija za TATA-vezujući protein
Bend17 A2|17 8.95 cMPočetak15,720,150 bp[2]
Kraj15,748,641 bp[2]
Obrazac RNK ekspresije
Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija• vezivanje sa DNK
• GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity
• transcription factor binding
• GO:0000980 RNA polymerase II cis-regulatory region sequence-specific DNA binding
• GO:0001948, GO:0016582 vezivanje za proteine
• vezivanje enzima
• TFIIB-class transcription factor binding
• aryl hydrocarbon receptor binding
• GO:0001158 cis-regulatory region sequence-specific DNA binding
• GO:0001200, GO:0001133, GO:0001201 DNA-binding transcription factor activity, RNA polymerase II-specific
• RNA polymerase III general transcription initiation factor activity
• GO:0000983 RNA polymerase II general transcription initiation factor activity
• RNA polymerase II core promoter sequence-specific DNA binding
• RNA polymerase III transcription regulatory region sequence-specific DNA binding
Ćelijska komponenta• citoplazma
• transcription factor TFIID complex
• male pronucleus
• female pronucleus
• nukleoplazma
• transcription factor TFIIA complex
• pronucleus
• jedro
• transcription preinitiation complex
• GO:0009327 makromolekulani kompleks
• transcription factor TFIIIB complex
• transcription regulator complex
Biološki proces• termination of RNA polymerase I transcription
• epigenetic maintenance of chromatin in transcription-competent conformation
• GO:0009373 regulation of transcription, DNA-templated
• transcription initiation from RNA polymerase I promoter
• transcription, DNA-templated
• GO:0060469, GO:0009371 positive regulation of transcription, DNA-templated
• Spermatogeneza
• DNA-templated transcription, initiation
• transcription initiation from RNA polymerase II promoter
• snRNA transcription by RNA polymerase II
• regulation of signal transduction by p53 class mediator
• GO:0022415 viral process
• regulation of transcription by RNA polymerase III
• transcription by RNA polymerase II
• transcription by RNA polymerase III
• RNA polymerase II preinitiation complex assembly
• GO:0044324, GO:0003256, GO:1901213, GO:0046019, GO:0046020, GO:1900094, GO:0061216, GO:0060994, GO:1902064, GO:0003258, GO:0072212 regulation of transcription by RNA polymerase II
• RNA polymerase III preinitiation complex assembly
• GO:0001183 transcription elongation from RNA polymerase I promoter
Izvori:Amigo / QuickGO
Ortolozi
VrsteČovjekMiš
Entrez

6908

21374

Ensembl

ENSG00000112592

ENSMUSG00000014767

UniProt

P20226

P29037

RefSeq (mRNK)

NM_003194
NM_001172085

NM_013684

RefSeq (bjelančevina)

NP_001165556
NP_003185

NP_038712

Lokacija (UCSC)Chr 6: 170.55 – 170.57 MbChr 17: 15.72 – 15.75 Mb
PubMed pretraga[3][4]
Wikipodaci
Pogledaj/uredi – čovjekPogledaj/uredi – miš
TBP
Kristalna struktura ternarnog kompleksa kvasca brf1-tbp-dnk
Identifikatori
SimbolTBP

TATA-vezujući protein (TBP) je opći transkripcijski faktor koji se veže za sekvencu DNK zvanu TATA-kutija. Ova sekvenca DNK nalazi se oko 30 baznih parova uzvodno od mjesta početka transkripcije u nekim eukariotskim genima promotorima.[5]

Aminokiselinska sekvenca

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|content=

style="font-family:monospace;"

10 20 30 40 50
MDQNNSLPPY AQGLASPQGA MTPGIPIFSP MMPYGTGLTP QPIQNTNSLS
ILEEQQRQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQAVAAA
AVQQSTSQQA TQGTSGQAPQ LFHSQTLTTA PLPGTTPLYP SPMTPMTPIT
PATPASESSG IVPQLQNIVS TVNLGCKLDL KTIALRARNA EYNPKRFAAV
IMRIREPRTT ALIFSSGKMV CTGAKSEEQS RLAARKYARV VQKLGFPAKF
LDFKIQNMVG SCDVKFPIRL EGLVLTHQQF SSYEPELFPG LIYRMIKPRI
VLLIFVSGKV VLTGAKVRAE IYEAFENIYP ILKGFRKTT

Porodica gena TBP

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TBP je član male porodice gena faktora povezanih s TBP-om.[6] Prvi faktor povezan s TBP-om (TRF/TRF1) identificiran je kod voćne mušice Drosophila, ali čini se da je specifičan za muhu ili insekte. Naknadno je TBPL1/TRF2 pronađen u genomima mnogih metazoa, dok genomi kičmenjaka kodiraju trećeg člana kičmenjačke porodice, TBPL2/TRF3. U specifičnim tipovima ćelija ili na specifičnim promotorima, TBP se može zamijeniti jednim od ovih faktora povezanih s TBP-om, od kojih neki interaguju s TATA-kutijom slično kao TBP.

Uloga kao transkripcijskog faktora

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TBP je podjedinica eukariotskog općeg transkripcijskog faktora TFIID. TFIID je prvi protein koji se veže za DNK tokom formiranja transkripcijskog preinicijacijskog kompleksa RNK-polimeraze II (RNK Pol II).[7] Kao jedan od rijetkih proteina u preinicijacijskom kompleksu koji se veže za DNK na način specifičan za sekvencu, pomaže u pozicioniranju RN-polimeraze II preko mjesta početka transkripcije gena. Međutim, procjenjuje se da samo 10–20% ljudskih promotora ima TATA kutije – većina ljudskih promotora su TATA-bez domaćinskog gena promotori – tako da TBP vjerovatno nije jedini protein uključen u pozicioniranje RNK-polimeraze II. Vezivanje TBP-a za ove promotore olakšavaju regulatori domaćinskog gena.[8][9] Zanimljivo je da transkripcija započinje unutar uske regije na oko 30 bp nizvodno od TATA-kutije, na promotorima koji sadrže TATA,[10] dok su mjesta početka transkripcije promotora bez TATA raspršena unutar regije od 200 bp.[9][11]

Vezivanje TFIID-a za TATA-kutiju u promotorskoj regiji gena inicira regrutovanje drugih faktora potrebnih da RNK Pol II započne transkripciju. Neki od ostalih regrutovanih transkripcijskih faktora uključuju TFIIA, TFIIB i TFIIF. Svaki od ovih transkripcijskih faktora sadrži nekoliko proteinskih podjedinica.

TBP je također važan za transkripciju putem RNK-polimeraze I i RNK polimeraze III, te je stoga uključen u inicijaciju transkripcije putem sve tri RNK- polimeraze.[12]

TBP je uključen u topljenje DNK (razdvajanje dvostrukog lanca) savijanjem DNK za 80° (sekvenca bogata AT-om na koju se veže olakšava lahko topljenje). TBP je neobičan protein po tome što se veže za manji žlijeb koristeći β list.

Još jedno karakteristično obilježje TBP-a je dugi niz glutamina na N-kraju proteina. Ova regija modulira aktivnost vezivanja DNK na C-terminalu, a modulacija vezivanja DNK utiče na brzinu formiranja transkripcijskog kompleksa i inicijaciju transkripcije. Mutacije koje proširuju broj CAG ponavljanja koja kodiraju ovaj poliglutaminski trakt, i time povećavaju dužinu poliglutaminskog niza, povezane su sa spinocerebelumskom ataksijom 17, neurodegenerativnim poremećajem klasifikovanim kao bolest poliglutamina.[13]

Interakcije DNK-protein

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Kada se TBP veže za TATA kutiju unutar DNK, on iskrivljuje DNK umetanjem aminokiselinakih bočnih lanaca između baznih parova, djelomično odmotavajući spiralu i dvostruko je savijajući. Iskrivljavanje se postiže velikom količinom površinskog kontakta između proteina i DNK. TBP se veže za negativno nabijene fosfate u DNK okosnici putem pozitivno nabijenih ostataka aminokiselina lizin i arginin. Oštro savijanje DNK nastaje projekcijom četiri glomazna ostatka fenilalanina u manji žlijeb. Kako se DNK savija, njen kontakt sa TBP-om se povećava, čime se pojačava interakcija DNK-protein.

Naprezanje nametnuto DNK kroz ovu interakciju inicira topljenje ili razdvajanje lanaca. Budući da je ova regija DNK bogata ostacima adenina i timina, koji se bazno sparuju putem samo dvije vodikove veze, lanci DNK se lakše razdvajaju. Razdvajanje dva lanca otkriva baze i omogućava RNK-polimerazi II da započne transkripciju gena.

C-terminalni dio TBP-a ima helikoidni oblik koji (nepotpuno) komplementira T-A-T-A regiju DNK. Ova nepotpunost omogućava DNK da se pasivno veže.

Za informacije o upotrebi TBP-a u ćelijama pogledajte: RNK-polimeraza I, RNK-polimeraza II i RNK-polimeraza III.

Interakcije protein-protein

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Pokazano je da protein koji veže TATA interraguje sa:

Složeno sastavljanje

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TATA-kutija veže protein (TBP) je potreban za inicijaciju transkripcije pomoću RNK polimeraza I, II i III, iz promotora sa ili bez TATA-kutije.[51][52] U prisustvu promotora bez TATA, TBP se veže uz pomoć faktora povezanih s TBP-om (TAF).[53][54] TBP se povezuje s mnoštvom faktora, uključujući opće transkripcijske faktore TFIIA, -B, -D, -E i -H, formirajući ogromne više-podjedinične preinicijacijske komplekse na jezgru promotora. Kroz svoju povezanost s različitim transkripcijskim faktorima, TBP može inicirati transkripciju iz različitih RNK-polimeraza. Postoji nekoliko srodnih TBP-ova, uključujući TBP-slične (TBPL) proteine.[55]

Struktura

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C-terminalno jezgro TBP-a (~180 ostataka) je visoko konzervirano i sadrži dva tandemska ponavljanja od 88 aminokiselina ponovljenja koja proizvode sedlastu strukturu koja se proteže preko DNK; ova regija vezuje se za TATA kutiju i interraguje sa transkripcijskim faktorima i regulatornim proteinima.[56] Nasuprot tome, N-terminalna regija varira i po dužini i po sekvenci.

Reference

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  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000112592 - Ensembl, maj 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000014767 - Ensembl, maj 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ Kornberg RD (2007). "The molecular basis of eukaryotic transcription". Proc. Natl. Acad. Sci. U.S.A. 104 (32): 12955–61. Bibcode:2007PNAS..10412955K. doi:10.1073/pnas.0704138104. PMC 1941834. PMID 17670940.
  6. ↑ Akhtar W, Veenstra GJ (1. 1. 2011). "TBP-related factors: a paradigm of diversity in transcription initiation". Cell & Bioscience. 1 (1): 23. doi:10.1186/2045-3701-1-23. PMC 3142196. PMID 21711503.
  7. ↑ Lee TI, Young RA (2000). "Transcription of eukaryotic protein-coding genes". Annual Review of Genetics. 34: 77–137. doi:10.1146/annurev.genet.34.1.77. PMID 11092823.
  8. ↑ Lam KC, Mühlpfordt F, Vaquerizas JM, Raja SJ, Holz H, Luscombe NM, Manke T, Akhtar A (2012). "The NSL complex regulates housekeeping genes in Drosophila". PLOS Genetics. 8 (6). doi:10.1371/journal.pgen.1002736. PMC 3375229. PMID 22723752.
  9. 1 2 Lam KC, Chung HR, Semplicio G, Iyer SS, Gaub A, Bhardwaj V, Holz H, Georgiev P, Akhtar A (februar 2019). "The NSL complex-mediated nucleosome landscape is required to maintain transcription fidelity and suppression of transcription noise". Genes & Development. 33 (7–8): 452–465. doi:10.1101/gad.321489.118. PMC 6446542. PMID 30819819.
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  31. ↑ Léveillard T, Wasylyk B (decembar 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.
  32. ↑ Shetty S, Takahashi T, Matsui H, Ayengar R, Raghow R (maj 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.
  33. ↑ Zhang H, Hu G, Wang H, Sciavolino P, Iler N, Shen MM, Abate-Shen C (maj 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 232144. PMID 9111364.
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  39. ↑ Guermah M, Malik S, Roeder RG (juni 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 108905. PMID 9584164.
  40. ↑ Schmitz ML, Stelzer G, Altmann H, Meisterernst M, Baeuerle PA (mart 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.
  41. ↑ 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. Bibcode:1995PNAS...92.8288S. doi:10.1073/pnas.92.18.8288. PMC 41142. PMID 7667283.
  42. ↑ Siegert JL, Robbins PD (januar 1999). "Rb inhibits the intrinsic kinase activity of TATA-binding protein-associated factor TAFII250". Mol. Cell. Biol. 19 (1): 846–54. doi:10.1128/MCB.19.1.846. PMC 83941. PMID 9858607.
  43. 1 2 3 4 Ruppert S, Wang EH, Tjian R (mart 1993). "Cloning and expression of human TAFII250: a TBP-associated factor implicated in cell-cycle regulation". Nature. 362 (6416): 175–9. Bibcode:1993Natur.362..175R. doi:10.1038/362175a0. PMID 7680771. S2CID 4364676.
  44. ↑ O'Brien T, Tjian R (maj 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.
  45. 1 2 3 Pointud JC, Mengus G, Brancorsini S, Monaco L, Parvinen M, Sassone-Corsi P, Davidson I (maj 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. S2CID 24519687.
  46. ↑ Tao Y, Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder RG (mart 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.
  47. ↑ Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (oktobar 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.
  48. 1 2 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. doi:10.1002/j.1460-2075.1995.tb07138.x. PMC 398239. PMID 7729427.
  49. ↑ May M, Mengus G, Lavigne AC, Chambon P, Davidson I (juni 1996). "Human TAF(II28) promotes transcriptional stimulation by activation function 2 of the retinoid X receptors". EMBO J. 15 (12): 3093–104. doi:10.1002/j.1460-2075.1996.tb00672.x. PMC 450252. PMID 8670810.
  50. ↑ Hoffmann A, Roeder RG (juli 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.
  51. ↑ Hochheimer A, Tjian R (juni 2003). "Diversified transcription initiation complexes expand promoter selectivity and tissue-specific gene expression". Genes & Development. 17 (11): 1309–20. doi:10.1101/gad.1099903. PMID 12782648.
  52. ↑ Pugh BF (septembar 2000). "Control of gene expression through regulation of the TATA-binding protein". Gene. 255 (1): 1–14. doi:10.1016/s0378-1119(00)00288-2. PMID 10974559.
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  55. ↑ Davidson I (juli 2003). "The genetics of TBP and TBP-related factors". Trends in Biochemical Sciences. 28 (7): 391–8. doi:10.1016/S0968-0004(03)00117-8. PMID 12878007.
  56. ↑ Nikolov DB, Hu SH, Lin J, Gasch A, Hoffmann A, Horikoshi M, Chua NH, Roeder RG, Burley SK (novembar 1992). "Crystal structure of TFIID TATA-box binding protein". Nature. 360 (6399): 40–6. Bibcode:1992Natur.360...40N. doi:10.1038/360040a0. PMID 1436073. S2CID 4307043.

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