E1A-dependent trans-activation of the c-fos promoter requires the TATAA sequence.

Simon, M. Celeste; Rooney, Robert J.; Fisch, T M; Heintz, Nathaniel; Nevins, Joseph R.

doi:10.1073/pnas.87.2.513

Cited by 51 publications

(33 citation statements)

References 53 publications

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“…A number of previous observations have also suggested this idea. For example, several studies have shown that different TATA boxes do not function similarly in the context of a given promoter, suggesting that the primary sequence of the TATA box and/or flanking sequences is important (Harbury and Struhl 1989;Simon et al 1990;Taylor and Kingston 1990;Wefald et al 1990;Li and Sherman 1991).…”

Section: Discussionmentioning

confidence: 99%

SPT3 interacts with TFIID to allow normal transcription in Saccharomyces cerevisiae.

Eisenmann¹,

Arndt²,

Ricupero³

et al. 1992

Genes Dev.

212

242

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Mutations in the Saccharomyces cerevisiae gene SPT15, which encodes the TATA-binding protein TFIID, have been shown to cause pleiotropic phenotypes and to lead to changes in transcription in vivo. Here, we report the cloning and analysis of one such mutation, sptl5-21, which causes a single-amino-acid substitution in a conserved residue of TFIID. Surprisingly, the sptl5-21 mutation does not affect the stability of TFIID, its ability to bind to DNA or to support basal transcription in vitro, or the ability of an upstream activator to function in vivo. To study further the sptlS-21 defect, extragenic suppressors of this mutation were isolated and analyzed. All of the extragenic suppressors of sptlS-21 are mutations in the previously identified SPT3 gene. Suppression of sptlS-21 by these spt3 mutations is allele-specific, suggesting that TFIID and SPT3 interact and that sptl5-21 impairs this interaction in some way. Consistent with these genetic data, coimmunoprecipitation experiments demonstrate that the TFIID and SPT3 proteins are physically associated in yeast extracts. Taken together, these results suggest that SPT3 is a TFIID-associated protein, required for TFIID to function at particular promoters in vivo.[ Transcription initiation by RNA polymerase II is a complicated process requiring the formation of a multicomponent, preinitiation complex near the start site of transcription (for review, see Sawadogo and Sentenac 1990;Roeder 1991). This complex is composed of a large number of proteins, including RNA polymerase II and several general transcription factors. These general factors were originally identified by fractionation of HeLa cell nuclear extracts into a number of activities essential for the accurate initiation of transcription by RNA polymerase II in vitro (Matsui et al. 1980;Samuels et al. 1982;Davison et al. 1983). At least some of these general factors have been identified in other eukaryotic systems, including Saccharomyces cerevisiae (Buratowski et al. 1988;Cavallini et al. 1988;Hahn et al. 1989a), Drosophila melanogaster (Wampler et al. 1990), and rat (Conaway and Conaway 1991), indicating that many components of the RNA polymerase II transcription machinery have been evolutionarily conserved.One of the general factors, TFIID, is believed to begin formation of the preinitiation complex by binding to the TATA box (Sawadogo and Roeder 1985b;Reinberg et al.

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Section: Discussionmentioning

confidence: 99%

SPT3 interacts with TFIID to allow normal transcription in Saccharomyces cerevisiae.

Eisenmann¹,

Arndt²,

Ricupero³

et al. 1992

Genes Dev.

212

242

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“…This high level of ICP4 induction was primarily determined by the low level of basal expression measured with this TATA box. Low basal expression with this TATA box has been observed in other studies (58,65,68). Further studies are required to determine if this low basal expression is due to low affinity for TBP and/or TFIID or to other factors.…”

Section: Discussionmentioning

confidence: 88%

“…1B). We chose TATA boxes derived from the SV40 early and adenovirus EIIa early promoters because these TATA boxes have previously been shown to elicit different degrees of induction by activator proteins, including E1a and large T antigen, compared with other consensus and nonconsensus TATA boxes (27,58,64,65). The HSV U L 39 TATA box was chosen because its promoter has been reported to be unresponsive to ICP4 (17 and references therein).…”

Section: Resultsmentioning

confidence: 99%

“…ICP4, E1a, and large T antigen are activators of gene expression whose activities display many similar characteristics, including the following: (i) specific DNA binding does not appear to be essential for activation (4,23,29,30,44,66), and (ii) each protein can activate simple promoters, some of which contain only a TATA box (29,30,65,71). We chose the SV40 and EIIa TATA boxes for our study of ICP4 in part because the responses of these TATA boxes to E1a and large T antigen have previously been analyzed.…”

Section: Discussionmentioning

confidence: 99%

“…The mechanisms by which activator proteins induce gene expression in the absence of specific DNA binding are poorly understood. However, some viral regulatory proteins that function independently of specific DNA binding require only a TATA box for induction (28,65,71). Moreover, E1a (36,48) and large T antigen (29) bind directly to either TFIID or more specifically the TATA-box-binding protein (TBP) component of TFIID, further implicating the TATA box as a common target for some viral activators.…”

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confidence: 99%

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Induction of Transcription by a Viral Regulatory Protein Depends on the Relative Strengths of Functional TATA Boxes

Cook

DeLuca

et al. 1995

Molecular and Cellular Biology

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The mechanisms by which viral regulatory proteins activate the cellular transcription apparatus without binding to specific DNA elements are not fully understood. Several lines of evidence suggest that activation by one such regulatory protein, herpes simplex virus ICP4, could be mediated, at least in part, by TFIID. To test this model, we replaced the TATA box of the ICP4-responsive viral thymidine kinase gene with functional TATA boxes that displayed different apparent affinities for TATA-box-binding protein as measured by DNase I footprinting. We measured the effects of these TATA boxes on ICP4 induction by constructing ICP4-deficient recombinant viruses containing the different TATA alleles and comparing their expression in cells lacking or expressing ICP4. Overall, ICP4 induced weak TATA boxes (those that displayed low apparent affinity for TATA-box-binding protein and low basal expression) the most (18-to 41-fold) and strong TATA boxes the least (7-to 10-fold). Therefore, ICP4 induction correlated inversely with TATA box strength. Using a reconstituted in vitro transcription assay, we determined that the relative levels of induction by ICP4 of the different TATA alleles were similar to those measured in vivo, suggesting that ICP4 was the only viral protein required for induction. These results fit a model in which ICP4 acts in part to enhance binding of TFIID to the TATA box. We compare and contrast these results with those observed with the viral regulatory proteins adenovirus E1a and simian virus 40 large T antigen and the cellular coactivator PC4.RNA polymerase II (pol II) promoters can roughly be separated into two functional elements: (i) proximal or core elements that consist of the TATA box and the transcriptional start site, and (ii) distal elements such as activator elements and enhancers. Numerous studies investigating the structures and functions of pol II promoters have provided a model in which the regulated expression of eukaryotic genes occurs through the interaction of the core elements which bind the basal transcription factors, including TFIID, TFIIB, TFIIA, TFIIE, TFIIF, TFIIG/J, and TFIIH (6, 10), and the distal elements which bind a wide variety of regulatory proteins such as Sp1 (for reviews, see references 50 and 52). However, some well-studied viral regulatory proteins, including adenovirus E1a, simian virus 40 (SV40) large T antigen, and herpes simplex virus (HSV) ICP4, can activate many genes without sequence-specific binding to DNA and independent of distal regulatory elements (4,23,29,30,38,44,71). This finding indicates that gene induction by activator proteins can involve mechanisms that are independent of specific DNA binding. The mechanisms by which activator proteins induce gene expression in the absence of specific DNA binding are poorly understood. However, some viral regulatory proteins that function independently of specific DNA binding require only a TATA box for induction (28,65,71). Moreover, E1a (36,48) and large T antigen (29) bind directly to either TFIID or more ...

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The interactions of transcription factors and their adaptors, coactivators and accessory proteins

Martin

1991

BioEssays

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Consistent with the complexity of the temporally regulated processes that must occur for growth and development of higher eukaryotes, it is now apparent that transcription is regulated by the formation of multicomponent complexes that assemble on the promoters of genes. These complexes can include (in addition to the five or more general transcription factors and RNA polymerase II) DNA-binding proteins, transcriptional activators, coactivators, adaptors and various accessory proteins. The best studied example of a complex that includes a transcriptional adaptor, accessory proteins and a DNA-binding protein is that involving the herpes simplex virus VP16 protein. Evidence suggests that the adenovirus E1a protein and the cellular Sp1 and CTF/NF1 transcription factors also function through adaptors or coactivators. Each additional component of the transcription complex provides the cell with another point at which to exert control of gene expression.

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E1A-dependent trans-activation of the c-fos promoter requires the TATAA sequence.

Abstract: Previous experiments have demonstrated

Cited by 51 publications

References 53 publications

SPT3 interacts with TFIID to allow normal transcription in Saccharomyces cerevisiae.

SPT3 interacts with TFIID to allow normal transcription in Saccharomyces cerevisiae.

Induction of Transcription by a Viral Regulatory Protein Depends on the Relative Strengths of Functional TATA Boxes

The interactions of transcription factors and their adaptors, coactivators and accessory proteins

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