TAF4

TAF4 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 135kDa, also known as TAF4, is a human gene.cite web | title = Entrez Gene: TAF4 TAF4 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 135kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6874| accessdate = ]

PBB_Summary
section_title =
summary_text = Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes one of the larger subunits of TFIID that has been shown to potentiate transcriptional activation by retinoic acid, thyroid hormone and vitamin D3 receptors. In addition, this subunit interacts with the transcription factor CREB, which has a glutamine-rich activation domain, and binds to other proteins containing glutamine-rich regions. Aberrant binding to this subunit by proteins with expanded polyglutamine regions has been suggested as one of the pathogenetic mechanisms underlying a group of neurodegenerative disorders referred to as polyglutamine diseases.cite web | title = Entrez Gene: TAF4 TAF4 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 135kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6874| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Zhou Q, Sharp PA |title=Novel mechanism and factor for regulation by HIV-1 Tat. |journal=EMBO J. |volume=14 |issue= 2 |pages= 321–8 |year= 1995 |pmid= 7835343 |doi=
*cite journal | author=Parada CA, Yoon JB, Roeder RG |title=A novel LBP-1-mediated restriction of HIV-1 transcription at the level of elongation in vitro. |journal=J. Biol. Chem. |volume=270 |issue= 5 |pages= 2274–83 |year= 1995 |pmid= 7836461 |doi=
*cite journal | author=Ou SH, Garcia-Martínez LF, Paulssen EJ, Gaynor RB |title=Role of flanking E box motifs in human immunodeficiency virus type 1 TATA element function. |journal=J. Virol. |volume=68 |issue= 11 |pages= 7188–99 |year= 1994 |pmid= 7933101 |doi=
*cite journal | author=Kashanchi F, Piras G, Radonovich MF, "et al." |title=Direct interaction of human TFIID with the HIV-1 transactivator tat. |journal=Nature |volume=367 |issue= 6460 |pages= 295–9 |year= 1994 |pmid= 8121496 |doi= 10.1038/367295a0
*cite journal | author=Wang Z, Morris GF, Rice AP, "et al." |title=Wild-type and transactivation-defective mutants of human immunodeficiency virus type 1 Tat protein bind human TATA-binding protein in vitro. |journal=J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. |volume=12 |issue= 2 |pages= 128–38 |year= 1996 |pmid= 8680883 |doi=
*cite journal | author=Pendergrast PS, Morrison D, Tansey WP, Hernandez N |title=Mutations in the carboxy-terminal domain of TBP affect the synthesis of human immunodeficiency virus type 1 full-length and short transcripts similarly. |journal=J. Virol. |volume=70 |issue= 8 |pages= 5025–34 |year= 1996 |pmid= 8764009 |doi=
*cite journal | author=Kashanchi F, Khleif SN, Duvall JF, "et al." |title=Interaction of human immunodeficiency virus type 1 Tat with a unique site of TFIID inhibits negative cofactor Dr1 and stabilizes the TFIID-TFIIA complex. |journal=J. Virol. |volume=70 |issue= 8 |pages= 5503–10 |year= 1996 |pmid= 8764062 |doi=
*cite journal | author=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. |journal=Science |volume=274 |issue= 5287 |pages= 605–10 |year= 1996 |pmid= 8849451 |doi=
*cite journal | author=Tanese N, Saluja D, Vassallo MF, "et al." |title=Molecular cloning and analysis of two subunits of the human TFIID complex: hTAFII130 and hTAFII100. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 24 |pages= 13611–6 |year= 1997 |pmid= 8942982 |doi=
*cite journal | author=García-Martínez LF, Ivanov D, Gaynor RB |title=Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 6951–8 |year= 1997 |pmid= 9054383 |doi=
*cite journal | author=Mengus G, May M, Carré L, "et al." |title=Human TAF(II)135 potentiates transcriptional activation by the AF-2s of the retinoic acid, vitamin D3, and thyroid hormone receptors in mammalian cells. |journal=Genes Dev. |volume=11 |issue= 11 |pages= 1381–95 |year= 1997 |pmid= 9192867 |doi=
*cite journal | author=Saluja D, Vassallo MF, Tanese N |title=Distinct subdomains of human TAFII130 are required for interactions with glutamine-rich transcriptional activators. |journal=Mol. Cell. Biol. |volume=18 |issue= 10 |pages= 5734–43 |year= 1998 |pmid= 9742090 |doi=
*cite journal | author=Brand M, Yamamoto K, Staub A, Tora L |title=Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction. |journal=J. Biol. Chem. |volume=274 |issue= 26 |pages= 18285–9 |year= 1999 |pmid= 10373431 |doi=
*cite journal | author=Inada A, Someya Y, Yamada Y, "et al." |title=The cyclic AMP response element modulator family regulates the insulin gene transcription by interacting with transcription factor IID. |journal=J. Biol. Chem. |volume=274 |issue= 30 |pages= 21095–103 |year= 1999 |pmid= 10409662 |doi=
*cite journal | author=Gangloff YG, Werten S, Romier C, "et al." |title=The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs. |journal=Mol. Cell. Biol. |volume=20 |issue= 1 |pages= 340–51 |year= 2000 |pmid= 10594036 |doi=
*cite journal | author=Brand M, Moggs JG, Oulad-Abdelghani M, "et al." |title=UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation. |journal=EMBO J. |volume=20 |issue= 12 |pages= 3187–96 |year= 2001 |pmid= 11406595 |doi= 10.1093/emboj/20.12.3187
*cite journal | author=Martinez E, Palhan VB, Tjernberg A, "et al." |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 |year= 2001 |pmid= 11564863 |doi= 10.1128/MCB.21.20.6782-6795.2001
*cite journal | author=Guermah M, Tao Y, Roeder RG |title=Positive and negative TAF(II) functions that suggest a dynamic TFIID structure and elicit synergy with traps in activator-induced transcription. |journal=Mol. Cell. Biol. |volume=21 |issue= 20 |pages= 6882–94 |year= 2001 |pmid= 11564872 |doi= 10.1128/MCB.21.20.6882-6894.2001
*cite journal | author=Felinski EA, Quinn PG |title=The coactivator dTAF(II)110/hTAF(II)135 is sufficient to recruit a polymerase complex and activate basal transcription mediated by CREB. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 23 |pages= 13078–83 |year= 2001 |pmid= 11687654 |doi= 10.1073/pnas.241337698
*cite journal | author=Deloukas P, Matthews LH, Ashurst J, "et al." |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865–71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a

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