Altered promoter binding of the TATA box-binding factor induced by the transcriptional activation domain of VP16 and suppressed by TF11A

Liljelund, Patricia; Cj, Ingles; Greenblatt, Jack

doi:10.1007/bf00279913

Cited by 11 publications

(7 citation statements)

References 40 publications

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“…In addition, the VP16 activation domain inhibits partially the TBP-TATA interaction, which is mediated by the concave face of TBP. It should be noted that inhibition of the TBP-TATA interaction and͞or TBP-mediated transcription by some activators has been reported by several groups (9,33), but the possibility that this effect could be due to activator interactions with the concave face of TBP has not previously been recognized.…”

Section: Discussionmentioning

confidence: 99%

Drosophila TAF _II 230 and the transcriptional activator VP16 bind competitively to the TATA box-binding domain of the TATA box-binding protein

Nishikawa

Kokubo

Horikoshi

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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The transcription initiation factor TFIID, consisting of the TATA box-binding protein (TBP) and many TBP-associated factors (TAFs), plays a central role in both basal and activated transcription. An intriguing finding is that the 80-residue N-terminal region of Drosophila TAF II 230 [dTAF II 230-(2-81)] can bind directly to TBP and inhibit its function. Here, studies with mutated forms of TBP demonstrate that dTAF II 230-(2-81) binds to the concave surface of TBP, which is important for TATA box binding. Previously, it was reported that a point mutation (L114K) on this concave surface destroys the ability of TBP to bind VP16 and to mediate VP16-dependent activation in vitro, but has no effect on basal transcription. Importantly, the same TBP mutation eliminates TBP binding to dTAF II 230-(2-81). Consistent with these effects of the L114K mutation, dTAF II 230-(2-81) and the VP16 activation domain compete for binding to wild-type TBP. These results indicate that transcriptional regulation may involve, in part, competitive interactions between transcriptional activators and TAFs on the TBP surface.Transcriptional initiation of eukaryotic protein-encoding genes requires at least six transcription initiation factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIIH) in addition to RNA polymerase II, and biochemical analyses with separated factors have defined a sequence of steps which lead to the in vitro formation of a preinitiation complex on a TATA box-containing promoter (reviewed in ref. 1). The first step is TFIID binding, a process that may be facilitated by TFIIA. The subsequent binding of TFIIB, through specific TATA box-binding protein (TBP) and DNA contacts, creates a platform that is in turn recognized by a complex consisting of RNA polymerase II and TFIIF. Further incorporation of TFIIE and TFIIH completes preinitiation complex formation. More recent studies have revealed complexes of RNA polymerase II, general initiation factors, and cofactors that may enter the preinitiation complex as a preassembled unit (reviewed in refs. 2 and 3). Because variable compositions of general factors have been reported for these holoenzyme complexes, depending upon both the species and the preparation methods, the assembly pathway most relevant to the in vivo situation remains unclear. However, TFIID binding to the promoter could be a critical checkpoint for promoter activation in several different pathways, consistent with studies showing both qualitative and quantitative effects of activators on TFIID binding (4 -11).TFIID itself is a multimeric protein complex consisting of TBP and TBP-associated factors (TAFs) whose sizes range from M r Ϸ 10,000 to Ͼ200,000 (for a review, see ref. TAFs also play an important role in promoter selectivity in basal transcription. Our earlier experiments with partially purified TFIID demonstrated that TFIID binds stably to a specific core promoter in a manner that depends on both the TATA and the downstream initiator-like elements (15). Deletion of the downstream element significant...

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Section: Discussionmentioning

confidence: 99%

Drosophila TAF _II 230 and the transcriptional activator VP16 bind competitively to the TATA box-binding domain of the TATA box-binding protein

Nishikawa

Kokubo

Horikoshi

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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“…The potent transactivation domain of VP16 enhances transcription from the promoter by multiple ways- 1) by recruiting 38 and stabilizing 39 the transcriptional machinery on the promoter by interacting with different transcriptional co-activators like TBP, TFIID, TFIIA, TFIIH 40–42 and with the Mediator (TRAP-SMCC-ARC) complex 43 2) by relieving nucleosome-mediated repression 44 and iii) by facilitating chromatin remodeling 45 . When the chimeric activator binds to Gal4-binding sites located upstream of the TATA box of a promoter they stimulate transcription in a synergistic fashion 45,46 .…”

Section: Discussionmentioning

confidence: 99%

Noninvasive Imaging of Therapeutic Gene Expression Using a Bidirectional Transcriptional Amplification Strategy

et al. 2008

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Tumor-specific promoters that limit transgene expression to tumors play a vital role in cancer gene therapy. Although tumor specific, the human Survivin promoter (pSurv) is a poor activator of transcription. A bi-directional Two Step Transcriptional Amplification (TSTA) system was designed to enhance expression of the therapeutic gene TNF-alpha Related Apoptosis Inducing Ligand (TRAIL or TR) and the reporter gene Firefly Luciferase (FL) from pSurv. An adenoviral vector carrying the enhanced targeting apparatus (Ad-pSurv-TR-G8-FL) was tested for efficiency and specificity of gene expression in cells and in living animals. Compared to the one-step systems (Ad-pSurv-FL or Ad-pSurv-TR), the bi-directional TSTA system showed 10-fold higher expression of both the therapeutic and the reporter gene and their expression correlated in cells (R2=0.99) and in animals (R2=0.67). Noninvasive quantitative monitoring of magnitude and time variation of TRAIL gene expression was feasible by bioluminescence imaging of the transcriptionally linked FL gene in xenograft tumors following intratumoral adenoviral injection. Moreover, the TSTA adenovirus maintained promoter specificity in non-target tissues following tail-vein administration. These studies demonstrate the potential of the bi-directional TSTA-system to achieve high levels of gene expression from a weak promoter, while preserving specificity and the ability to image expression of the therapeutic gene noninvasively.

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“…In many other cases, binding of a protein to a single binding site causes bending of DNA (49 -51). DNaseI footprinting studies with these proteins, however, revealed only a small number of hypersensitive sites, generally located within the area protected against cleavage (2,(52)(53)(54)(55)(56)(57)(58)(59)(60)(61)(62). DNaseI footprints of E. coli Lrp with several target promoter fragments show protection from DNaseI over a range of 100 bp or even longer, due to multiple binding sites.…”

Section: Fig 9 Sds-page Analysis Of Cross-linking Experiments Withmentioning

confidence: 99%

An Lrp-like Transcriptional Regulator from the ArchaeonPyrococcus furiosus Is Negatively Autoregulated

Brinkman¹,

Dahlke²,

Tuininga³

et al. 2000

Journal of Biological Chemistry

116

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The archaeal transcriptional initiation machinery closely resembles core elements of the eukaryal polymerase II system. However, apart from the established basal archaeal transcription system, little is known about the modulation of gene expression in archaea. At present, no obvious eukaryal-like transcriptional regulators have been identified in archaea. Instead, we have previously isolated an archaeal gene, the Pyrococcus furiosus lrpA, that potentially encodes a bacterial-like transcriptional regulator. In the present study, we have for the first time addressed the actual involvement of an archaeal Lrp homologue in transcription modulation. For that purpose, we have produced LrpA in Escherichia coli. In a cell-free P. furiosus transcription system we used wild-type and mutated lrpA promoter fragments to demonstrate that the purified LrpA negatively regulates its own transcription. In addition, gel retardation analyses revealed a single protein-DNA complex, in which LrpA appeared to be present in (at least) a tetrameric conformation. The location of the LrpA binding site was further identified by DNaseI and hydroxyl radical footprinting, indicating that LrpA binds to a 46-base pair sequence that overlaps the transcriptional start site of its own promoter. The molecular basis of the transcription inhibition by LrpA is discussed.Recent studies have revealed that the archaeal transcriptional machinery represents a simplified version of the eukaryal RNA polymerase II transcription apparatus, which involves homologues of the TATA-binding protein (TBP), 1 the transcription factor IIB (TFIIB; the archaeal homologue is called TFB), and the multi-subunit RNA polymerase II (for a recent review, see Ref. 1). The initiation process starts when the TBP interacts specifically with the core promoter element, the TATA box, which is located at positions Ϫ25 to Ϫ30 relative to the transcriptional start site (ϩ1). This complex is stabilized by TFB, which interacts with TBP as well as with the nucleotides Ϫ42 to Ϫ19 that flank the TATA box (2). In particular, a sequence upstream of the TATA box (called the TFB-responsive element or BRE) is essential for transcriptional polarity (3,4

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Altered promoter binding of the TATA box-binding factor induced by the transcriptional activation domain of VP16 and suppressed by TF11A

Cited by 11 publications

References 40 publications

Drosophila TAF _II 230 and the transcriptional activator VP16 bind competitively to the TATA box-binding domain of the TATA box-binding protein

Drosophila TAF _II 230 and the transcriptional activator VP16 bind competitively to the TATA box-binding domain of the TATA box-binding protein

Noninvasive Imaging of Therapeutic Gene Expression Using a Bidirectional Transcriptional Amplification Strategy

An Lrp-like Transcriptional Regulator from the ArchaeonPyrococcus furiosus Is Negatively Autoregulated

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Altered promoter binding of the TATA box-binding factor induced by the transcriptional activation domain of VP16 and suppressed by TF11A

Cited by 11 publications

References 40 publications

Drosophila TAF II 230 and the transcriptional activator VP16 bind competitively to the TATA box-binding domain of the TATA box-binding protein

Drosophila TAF II 230 and the transcriptional activator VP16 bind competitively to the TATA box-binding domain of the TATA box-binding protein

Noninvasive Imaging of Therapeutic Gene Expression Using a Bidirectional Transcriptional Amplification Strategy

An Lrp-like Transcriptional Regulator from the ArchaeonPyrococcus furiosus Is Negatively Autoregulated

Contact Info

Product

Resources

About

Drosophila TAF _II 230 and the transcriptional activator VP16 bind competitively to the TATA box-binding domain of the TATA box-binding protein

Drosophila TAF _II 230 and the transcriptional activator VP16 bind competitively to the TATA box-binding domain of the TATA box-binding protein