TAF5

TAF5

TAF5 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 100kDa, also known as TAF5, is a human gene.cite web | title = Entrez Gene: TAF5 TAF5 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 100kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6877| 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 an integral subunit of TFIID associated with all transcriptionally competent forms of that complex. This subunit interacts strongly with two TFIID subunits that show similarity to histones H3 and H4, and it may participate in forming a nucleosome-like core in the TFIID complex.cite web | title = Entrez Gene: TAF5 TAF5 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 100kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6877| 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=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*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=Dubrovskaya V, Lavigne AC, Davidson I, "et al." |title=Distinct domains of hTAFII100 are required for functional interaction with transcription factor TFIIF beta (RAP30) and incorporation into the TFIID complex. |journal=EMBO J. |volume=15 |issue= 14 |pages= 3702–12 |year= 1996 |pmid= 8758937 |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=Dubrovskaya V, Mattei MG, Tora L |title=Localization of the gene (TAF2D) encoding the 100-kDa subunit (hTAFII100) of the human TFIID complex to chromosome 10 band q24-q25.2. |journal=Genomics |volume=36 |issue= 3 |pages= 556–7 |year= 1997 |pmid= 8884287 |doi= 10.1006/geno.1996.0509
*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=Tao Y, Guermah M, Martinez E, "et al." |title=Specific interactions and potential functions of human TAFII100. |journal=J. Biol. Chem. |volume=272 |issue= 10 |pages= 6714–21 |year= 1997 |pmid= 9045704 |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=Dantonel JC, Murthy KG, Manley JL, Tora L |title=Transcription factor TFIID recruits factor CPSF for formation of 3' end of mRNA. |journal=Nature |volume=389 |issue= 6649 |pages= 399–402 |year= 1997 |pmid= 9311784 |doi= 10.1038/38763
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Bertolotti A, Melot T, Acker J, "et al." |title=EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes. |journal=Mol. Cell. Biol. |volume=18 |issue= 3 |pages= 1489–97 |year= 1998 |pmid= 9488465 |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=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

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