A TATA Element Is Required for tRNA Promoter Activity and Confers TATA-binding Protein Responsiveness inDrosophilaSchneider-2 Cells

Quantitative characteristics of interaction recombinant TATA-binding protein (TBP) with oligonucleotides identical to natural TATA-containing promoter region genes of mammals are received. In particular, new experimental data about the importance guanine in 8-th position of the TATA-element for affinity to TBP are received. The experimental data, testifying that raised maintenance G and С nucleotides in flanks of TATA-element does the contribution to affinity to TBP are received.

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TFIIA Interacts with TFIID via Association with TATA-Binding Protein and TAF40

Molecular and Cellular Biology ◽

10.1128/mcb.21.5.1737-1746.2001 ◽

2001 ◽

Vol 21 (5) ◽

pp. 1737-1746 ◽

Cited By ~ 23

Author(s):

Susan M. Kraemer ◽

Ryan T. Ranallo ◽

Ryan C. Ogg ◽

Laurie A. Stargell

Keyword(s):

Transcription Factor ◽

Rna Polymerase Ii ◽

Functional Role ◽

Associated Factors ◽

Binding Protein ◽

Tata Binding Protein ◽

Functional Interaction ◽

General Transcription Factor ◽

Tata Element

ABSTRACT TFIIA and TATA-binding protein (TBP) associate directly at the TATA element of genes transcribed by RNA polymerase II. In vivo, TBP is complexed with approximately 14 TBP-associated factors (TAFs) to form the general transcription factor TFIID. How TFIIA and TFIID communicate is not well understood. We show that in addition to making direct contacts with TBP, yeast TAF40 interacts directly and specifically with TFIIA. Mutational analyses of the Toa2 subunit of TFIIA indicate that loss of functional interaction between TFIIA and TAF40 results in conditional growth phenotypes and defects in transcription. These results demonstrate that the TFIIA-TAF40 interaction is important in vivo and indicate a functional role for TAF40 as a bridging factor between TFIIA and TFIID.

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Contribution of sequences downstream of the TATA element to a protein-DNA complex containing the TATA-binding protein.

Molecular and Cellular Biology ◽

10.1128/mcb.13.4.2593 ◽

1993 ◽

Vol 13 (4) ◽

pp. 2593-2603 ◽

Cited By ~ 37

Author(s):

B A Purnell ◽

D S Gilmour

Keyword(s):

Binding Protein ◽

Core Promoter ◽

Tata Binding Protein ◽

Start Site ◽

Histone H4 ◽

Normal Core ◽

Tata Element ◽

Gel Shift Assay ◽

Dna Complex ◽

Made In

A TATA complex that forms on the hsp70 promoter has been found to depend on sequence-specific interactions that occur at the transcription start and regions further downstream. The complex was detected with a gel shift assay and further characterized with interference assays. Antibodies reveal that the TATA-binding protein is in the complex. Interference assays localize specific contacts in the TATA element, the start site, and in a region approximately 25 bp downstream of the start site that contribute to either the assembly or the maintenance of the complex. Contact at the TATA element is made in the minor groove, as has been reported for the recombinant TATA-binding protein. Mutation in the TATA element or the start site of hsp70 causes complex formation to be more strongly dependent on contacts in the +25 region than in the normal core promoter. Examination of the hsp26 and histone H4 genes indicates that similar contacts contribute to the TATA complexes that form on these promoters. The results suggest that specific contacts downstream of the TATA element could play a key role in establishing the transcriptional potential of a gene by contributing to the interaction of the TATA-binding protein.

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Differential regulation of MAGE-A1 promoter activity by BORIS and Sp1, both interacting with the TATA binding protein

BMC Cancer ◽

10.1186/1471-2407-14-796 ◽

2014 ◽

Vol 14 (1) ◽

Cited By ~ 9

Author(s):

Heidi Schwarzenbach ◽

Corinna Eichelser ◽

Bettina Steinbach ◽

Josefine Tadewaldt ◽

Klaus Pantel ◽

...

Keyword(s):

Promoter Activity ◽

Binding Protein ◽

Tata Binding Protein ◽

Differential Regulation

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Interdependent Interactions between TFIIB, TATA Binding Protein, and DNA

Molecular and Cellular Biology ◽

10.1128/mcb.22.24.8735-8743.2002 ◽

2002 ◽

Vol 22 (24) ◽

pp. 8735-8743 ◽

Cited By ~ 7

Author(s):

Robin M. Buratowski ◽

Jessica Downs ◽

Stephen Buratowski

Keyword(s):

Biochemical Characterization ◽

Binding Protein ◽

Tata Binding Protein ◽

Temperature Sensitive ◽

Hydrophobic Residues ◽

Step Model ◽

Tata Element ◽

Binding Surface ◽

Tbp Gene ◽

Dna Complex

ABSTRACT Temperature-sensitive mutants of TFIIB that are defective for essential interactions were isolated. One mutation (G204D) results in disruption of a protein-protein contact between TFIIB and TATA binding protein (TBP), while the other (K272I) disrupts an interaction between TFIIB and DNA. The TBP gene was mutagenized, and alleles that suppress the slow-growth phenotypes of the TFIIB mutants were isolated. TFIIB with the G204D mutation [TFIIB(G204D)] was suppressed by hydrophobic substitutions at lysine 239 of TBP. These changes led to increased affinity between TBP and TFIIB. TFIIB(K272I) was weakly suppressed by TBP mutants in which K239 was changed to hydrophobic residues. However, this mutant TFIIB was strongly suppressed by conservative substitutions in the DNA binding surface of TBP. Biochemical characterization showed that these TBP mutants had increased affinity for a TATA element. The TBPs with increased affinity could not suppress TFIIB(G204D), leading us to propose a two-step model for the interaction between TFIIB and the TBP-DNA complex.

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Simian Virus 40 Large T Antigen Stabilizes the TATA-Binding Protein–TFIIA Complex on the TATA Element

Molecular and Cellular Biology ◽

10.1128/mcb.18.7.3926 ◽

1998 ◽

Vol 18 (7) ◽

pp. 3926-3935 ◽

Cited By ~ 18

Author(s):

Blossom Damania ◽

Paul Lieberman ◽

James C. Alwine

Keyword(s):

Binding Protein ◽

Simian Virus 40 ◽

Simian Virus ◽

Tata Binding Protein ◽

T Antigen ◽

Early Gene ◽

Large T Antigen ◽

Complex Assembly ◽

Tata Element

ABSTRACT Large T antigen (T antigen), the early gene product of simian virus 40 (SV40), is a potent transcriptional activator of both cellular and viral genes. Recently we have shown that T antigen is tightly associated with TFIID and, in this position, performs a TATA-binding protein (TBP)-associated factor (TAF)-like function. Based on this observation, we asked whether T antigen affected steps in preinitiation complex assembly. Using purified components in in vitro complex assembly assays, we found that T antigen specifically enhances the formation of the TBP-TFIIA complex on the TATA element. T antigen accomplishes this by increasing the rate of formation of the TBP-TFIIA complex on the TATA element and by stabilizing the complexes after they are formed on the promoter. In addition, DNA immunoprecipitation experiments indicate that T antigen is associated with the stabilized TBP-TFIIA complexes bound to the DNA. In this regard, it has previously been shown that T antigen interacts with TBP; in the present study, we show that T antigen also interacts with TFIIA in vitro. In testing the ability of T antigen to stabilize the TBP-TFIIA complex, we found that stabilization is highly sensitive to the specific sequence context of the TATA element. Previous studies showed that T antigen could activate simple promoters containing the TATA elements from thehsp70 and c-fos gene promoters but failed to significantly activate similar promoters containing the TATA elements from the promoters of the SV40 early and adenovirus E2a genes. We find that the ability to stabilize the TBP-TFIIA complex on thehsp70 and c-fos TATA elements, and not on the SV40 early and E2A TATA elements, correlates with the ability or inability to activate promoters containing these TATA elements.

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TATA-Binding Protein–TATA Interaction Is a Key Determinant of Differential Transcription of Silkworm Constitutive and Silk Gland-Specific tRNAAla Genes

Molecular and Cellular Biology ◽

10.1128/mcb.20.4.1329-1343.2000 ◽

2000 ◽

Vol 20 (4) ◽

pp. 1329-1343 ◽

Cited By ~ 21

Author(s):

Ching Ouyang ◽

M. Juanita Martinez ◽

Lisa S. Young ◽

Karen U. Sprague

Keyword(s):

Promoter Activity ◽

Transcriptional Activity ◽

Binding Protein ◽

Tata Binding Protein ◽

Silk Gland ◽

Wild Type ◽

Heparin Resistance ◽

Transcription Complexes ◽

Differential Transcription

ABSTRACT We have investigated the contribution of specific TATA-binding protein (TBP)–TATA interactions to the promoter activity of a constitutively expressed silkworm tRNAC Ala gene and have also asked whether the lack of similar interactions accounts for the low promoter activity of a silk gland-specific tRNASG Ala gene. We compared TBP binding, TFIIIB-promoter complex stability (measured by heparin resistance), and in vitro transcriptional activity in a series of mutant tRNAC Ala promoters and found that specific TBP-TATA contacts are important for TFIIIB-promoter interaction and for transcriptional activity. Although the wild-type tRNAC Ala promoter contains two functional TBP binding sequences that overlap, the tRNASG Ala promoter lacks any TBP binding site in the corresponding region. This feature appears to account for the inefficiency of the tRNASG Alapromoter since provision of either of the wild-type TATA sequences derived from the tRNAC Ala promoter confers robust transcriptional activity. Transcriptional impairment of the wild-type tRNASG Ala gene is not due to reduced incorporation of TBP into transcription complexes since both the tRNAC Ala and tRNASG Ala promoters form transcription complexes that contain the same amount of TBP. Thus, the deleterious consequences of the lack of appropriate TBP-TATA contacts in the tRNASG Ala promoter must come from failure to incorporate some other essential transcription factor(s) or to stabilize the complete complex in an active conformation.

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A new class of activation-defective TATA-binding protein mutants: evidence for two steps of transcriptional activation in vivo.

Molecular and Cellular Biology ◽

10.1128/mcb.16.8.4456 ◽

1996 ◽

Vol 16 (8) ◽

pp. 4456-4464 ◽

Cited By ~ 34

Author(s):

L A Stargell ◽

K Struhl

Keyword(s):

Transcriptional Activation ◽

Binding Protein ◽

Tata Binding Protein ◽

Wild Type ◽

Protein Protein Interaction ◽

New Class ◽

Tata Element ◽

Protein Mutants ◽

Transcriptional Stimulation

Using a genetic screen, we isolated four TATA-binding protein (TBP) mutants that are specifically defective in vivo for the response to acidic activators. In contrast to previously described activation-defective TBP mutants, these TBP derivatives are not specifically defective for interactions with TATA elements or TFIIA. Three of these derivatives interact normally with a TATA element, TFIIA, TFIIB, or an acidic activation domain; presumably, they affect another protein-protein interaction important for transcriptional activation. The remaining derivative (with F-237 replaced by D) binds a TATA element with wild-type affinity, but the TBP-TATA complex has an altered electrophoretic mobility and interacts poorly with TFIIA and TFIIB; this suggests that the conformation of the TBP-TATA element complex plays a role in transcriptional activation. To determine the step at which the TBP derivatives were unable to activate transcription, we utilized an artificial recruitment assay in which TBP is targeted to the promoter via fusion to the LexA DNA-binding domain. Consistent with previous evidence that acidic activators can increase recruitment of TBP to the promoter in vivo, the activation defect of some of these TBP derivatives can be corrected by artificial recruitment. In contrast, the activation defect of the other TBP derivatives is not bypassed by artificial recruitment. Thus, these TBP mutants define two steps in the process of transcriptional stimulation by acidic activators: efficient recruitment to the TATA element and a postrecruitment interaction with a component(s) of the initiation complex.

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Transcriptional Regulation of the TATA-Binding Protein by Ras Cellular Signaling

Molecular and Cellular Biology ◽

10.1128/mcb.20.14.5000-5009.2000 ◽

2000 ◽

Vol 20 (14) ◽

pp. 5000-5009 ◽

Cited By ~ 27

Author(s):

Sandra A. S. Johnson ◽

Nihar Mandavia ◽

Horng-Dar Wang ◽

Deborah L. Johnson

Keyword(s):

Transcription Factor ◽

Promoter Activity ◽

Binding Protein ◽

Rat Hepatocytes ◽

Tata Binding Protein ◽

Mitogen Activated Protein Kinase ◽

Transcriptional Level ◽

Ras Signaling ◽

Dependent Manner ◽

X Protein

ABSTRACT Our previous studies have demonstrated that the level of the central transcription factor TATA-binding protein (TBP) is increased in cells expressing the hepatitis B virus (HBV) X protein through the activation of the Ras signaling pathway, which serves to enhance both RNA polymerase I and III promoter activities. To understand the mechanism by which TBP is regulated, we have investigated whether enhanced expression is modulated at the transcriptional level. Nuclear run-on assays revealed that the HBV X protein increases the number of active transcription complexes on the TBP gene. In transient-transfection assays with both transformed and primary hepatocytes, the human TBP promoter was shown to be induced by expression of the HBV X protein in a Ras-dependent manner, requiring both Ral guanine nucleotide dissociation stimulator (RalGDS) and Raf signaling. Transient overexpression of TBP did not affect TBP promoter activity. To further delineate the downstream Ras-mediated events contributing to TBP promoter regulation in primary rat hepatocytes, the best-characterized Ras effectors, Raf, phosphoinositide 3-kinase (PI-3 kinase), and RalGDS, were examined. Activation of either Raf or RalGDS, but not that of PI-3 kinase, was sufficient to induce TBP promoter activity. Both Raf- and RalGDS-mediated induction required the activation of mitogen-activated protein kinase kinase (MEK). In addition, another distinct Ras-activated pathway, which does not require MEK activation, appears to induce TBP promoter activity. Analysis of the DNA sequence requirement within the TBP promoter responsible for these regulatory events defined three distinct regions that modulate the abilities of Raf, RalGDS, and the Ras-dependent, MEK-independent pathways to regulate human TBP promoter activity. Together, these results provide new evidence that TBP can be regulated at the transcriptional level and identify three distinct Ras-activated pathways that modulate this central eukaryotic transcription factor.

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