Factors involved in specific transcription by mammalian RNA polymerase II: purification and analysis of transcription factor IIA and identification of transcription factor IIJ.

Cortés, Patricia; Flores, Osvaldo; Reinberg, Danny

doi:10.1128/mcb.12.1.413

Cited by 125 publications

(167 citation statements)

References 31 publications

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“…Our reconstituted in vitro transcription system consisted of the recombinant human general factors TBP (79), TFIIB (36), TFIIE (a and ,) (78), and TFIIF (RAP30 and RAP74) (24,99) all produced in E. coli; highly purified calf thymus RNA polymerase 11 (100); and the general initiation factor fractions TFIIA/TFIIJ (104) and TFIIH (26) partially purified from HeLa nuclear extracts. The TFIIA/TFIIJ fraction used in our experiments contained both TFIIA and TFIIJ, but only the TFIIJ activity is necessary for production of runoff transcripts from the adenovirus major late promoter in reactions involving recombinant TBP (14). As is shown in Fig.…”

Section: Interaction Of the Vp16 Activation Domain With Tfiihmentioning

confidence: 69%

“…Since the critical F442 residue of VP16 is outside the portion of VP16 that binds TAF40 and since point mutations in VP16 that affect both transactivation by VP16 and the binding to VP16 of TAF40 have yet to be described (30), the effects of VP16 point mutations on transactivation seem to correlate best VOL. 14,1994 on Yeast whole-cell extract that was prepared from strain BJ2168 as described previously (115) so far with their effects on the binding to VP16 of TFIID (TBP) and TFIIH (p62). It is unclear whether VP16 point mutations that affect activation have similar effects on the binding to VP16 of TBP and TFIIH because these general factors bind to VP16 in similar ways or because the VP16 point mutations affect the folding of the VP16 activation domain.…”

Section: Discussionmentioning

confidence: 99%

“…In contrast, an irrelevant monoclonal antibody against the retinoblastoma protein had no effect (lanes 16 and 17). Moreover, the inhibition by M.Ab3c9 was specific because it could be reversed by the addition to the reaction of excess TFIIH that had been highly purified by VP16 affinity chromatography and subsequent phosphocellulose chromatography (lanes 10 to 13) but not by the addition of excess TFIIB (lanes 14 and 15). Furthermore, when the affinity column eluates were subjected to Western blotting with M.Ab3c9, only the GST-VP16 column eluate, and not the control GST column eluate, contained the immunoreactive p62 polypeptide (Fig.…”

Section: Interaction Of the Vp16 Activation Domain With Tfiihmentioning

confidence: 99%

“…Beginning with TFIID, which recognizes the TATA boxes present in many promoters for RNA polymerase II, these factors and RNA polymerase II can be assembled in a defined order onto a promoter (5). TFIIH and TFIIJ are the last of these factors to bind to an assembling initiation complex (12,14,26), and TFIIH, also known as BTF2, is the only factor known to possess associated enzymatic activities. These include an ATP-dependent DNA helicase activity (95,96) and a protein kinase activity that can phosphorylate the carboxyterminal heptapeptide repeat domain (CTD) of the largest subunit of RNA polymerase 11 (12,21,68).…”

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confidence: 99%

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Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53.

Xiao¹,

Pearson²,

Coulombe³

et al. 1994

Mol. Cell. Biol.

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339

274

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Acidic transcriptional activation domains function well in both yeast and mammalian cells, and some have been shown to bind the general transcription factors TFIID and TFIIB. We now show that two acidic transactivators, herpes simplex virus VP16 and human p53, directly interact with the multisubunit human general transcription factor TFIHH and its Saccharomyces cerevisuze counterpart, factor b. The VP16-and p53-binding domains in these factors lie in the p62 subunit of TFIIH and in the homologous subunit, TFB1, of factor b. Point mutations in VP16 that reduce its transactivation activity in both yeast and mammalian cells weaken its binding to both yeast and human TFIIH. This suggests that binding of activation domains to TFIIH is an important aspect of transcriptional activation.Accurate transcription in vitro by human RNA polymerase II involves the general transcription factors TFIIA, TFIIB, TFIID, TFIIE, TFIIF (RAP30 and RAP74), TFIIH (also known as BTF2), and TFIIJ (reviewed in references 13 and 121). Beginning with TFIID, which recognizes the TATA boxes present in many promoters for RNA polymerase II, these factors and RNA polymerase II can be assembled in a defined order onto a promoter (5). TFIIH and TFIIJ are the last of these factors to bind to an assembling initiation complex (12,14,26), and TFIIH, also known as BTF2, is the only factor known to possess associated enzymatic activities. These include an ATP-dependent DNA helicase activity (95, 96) and a protein kinase activity that can phosphorylate the carboxyterminal heptapeptide repeat domain (CTD) of the largest subunit of RNA polymerase 11 (12, 21,68 herpes simplex virus transactivator VP16 (107) and in the N-terminal 73 amino acids of the mammalian tumor suppressor protein p53 (23). The p53 protein has a site-specific DNA-binding domain in its carboxy-terminal portion (101). VP16 does not, by itself, bind specifically to DNA, but instead its amino-terminal portion binds DNA in association with mammalian factors, including the POU homeodomain protein Oct-1 that recognizes octamer sequences in DNA (28,60,102). When fused to the DNA-binding domain of GAL4, the VP16 and p53 activation domains stimulate transcription in yeast and human cells of a gene bearing GAL4-binding sites (9,16,23,74,87,92). These observations imply that common mechanisms for transcriptional activation by acidic activators may exist in fungi and mammals.Many activation domains have been shown to interact with the TATA-box-binding protein (TBP) subunit of TFIID. These include the highly acidic activation domains in VP16 (50,103), p53 (10,67,72,84,97,108),118), and E2F-1 (37), as well as other kinds of activation domains found in the adenovirus activator ElA (48, 62), the Epstein-Barr virus proteins Zta (64) and R (70), the human T-cell leukemia virus type 1 (HTLV-1) activator Taxl (8), the transactivator Tat of human immunodeficiency virus type 1 (HIV-1) (53), and human c-Fos and c-Jun (85), PU-1 (38), and Spl (20). In certain cases, reduced binding of TBP by activation domains wit...

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Section: Interaction Of the Vp16 Activation Domain With Tfiihmentioning

confidence: 69%

Section: Discussionmentioning

confidence: 99%

Section: Interaction Of the Vp16 Activation Domain With Tfiihmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53.

Xiao¹,

Pearson²,

Coulombe³

et al. 1994

Mol. Cell. Biol.

Self Cite

339

274

View full text Add to dashboard Cite

show abstract

“…As a result, DSP1 displaces TFIIA, which inhibits recruitment of TFIIF-RNA pol II to the promoter. TFIIA also blocks access of other repressors to TBP [95,96], and therefore DSP1-mediated repression may be more complicated than is reported so far. Several other repressors, such as Dr1 [97] and Dr2 [98], interact with TBP to inhibit its association with TFIIA and TFIIB respectively, while others still have been shown to interact with TFIIB (unliganded thyroid hormone receptor [99,100]) and TFIIE (Kruppell gene [101]).…”

Section: Classical Silencers (Silencer Elements)mentioning

confidence: 89%

Transcriptional control and the role of silencers in transcriptional regulation in eukaryotes

Ogbourne

Antalis

1998

Biochemical Journal

227

171

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Mechanisms controlling transcription and its regulation are fundamental to our understanding of molecular biology and, ultimately, cellular biology. Our knowledge of transcription initiation and integral factors such as RNA polymerase is considerable, and more recently our understanding of the involvement of enhancers and complexes such as holoenzyme and mediator has increased dramatically. However, an understanding of transcriptional repression is also essential for a complete understanding of promoter structure and the regulation of gene expression. Transcriptional repression in eukaryotes is achieved through ‘silencers ’, of which there are two types, namely ‘silencer elements ’ and ‘negative regulatory elements ’ (NREs). Silencer elements are classical, position-independent elements that direct an active repression mechanism, and NREs are position-dependent elements that direct a passive repression mechanism. In addition, ‘repressors ’ are DNA-binding trasncription factors that interact directly with silencers. A review of the recent literature reveals that it is the silencer itself and its context within a given promoter, rather than the interacting repressor, that determines the mechanism of repression. Silencers form an intrinsic part of many eukaryotic promoters and, consequently, knowledge of their interactive role with enchancers and other transcriptional elements is essential for our understanding of gene regulation in eukaryotes.

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Randomly phosphorylated polystyrene derivatives interact with RNA polymerase II transcription factors: Part I

Imbert¹,

Letourneur

Jozéfowicz³

1997

J. Biomed. Mater. Res.

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Insoluble functional synthetic random copolymers are able to develop at their surfaces specific interactions with biologic components. Crosslinked phosphorylated polystyrene derivatives were previously shown to mimic DNA antigen because they interacted with anti-DNA antibodies found in the sera of systemic lupus erythematosus patients. These biospecific surfaces were postulated to be able to bind other DNA-binding proteins such as RNA polymerase II transcription factors. Indeed, these proteins play a major role in gene regulation in mammalian cells. This hypothesis was checked by adsorption and elution of HeLa cell nuclear extracts on a 72% phosphorylated resin. The composition of the eluted fractions were analyzed by electrophoresis, and the biologic activity of the transcription factors was tested using an in vitro transcription assay. The results showed that USF, TATA-binding protein (TBP), and TFIIB were specifically adsorbed on the polymer and that all eluted factors kept their biologic activity. Therefore, randomly phosphorylated polystyrene derivatives may be useful for the fractionation of RNA polymerase II transcription factors.

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Factors involved in specific transcription by mammalian RNA polymerase II: purification and analysis of transcription factor IIA and identification of transcription factor IIJ.

Cited by 125 publications

References 31 publications

Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53.

Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53.

Transcriptional control and the role of silencers in transcriptional regulation in eukaryotes

Randomly phosphorylated polystyrene derivatives interact with RNA polymerase II transcription factors: Part I

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