Drosophila 230-kD TFIID subunit, a functional homolog of the human cell cycle gene product, negatively regulates DNA binding of the TATA box-binding subunit of TFIID.

Kokubo, Tetsuro; Gong, Da-Wei; Yamashita, Shinya; Horikoshi, Masami; Roeder, Robert G.; Nakatani, Y.

doi:10.1101/gad.7.6.1033

Cited by 94 publications

(99 citation statements)

References 81 publications

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“…These findings are partly consistent with published results that have shown recombinant TAF II 230 can inhibit transcription in vitro (35,37). However, Kokubo et al (37) showed that TAF II 230 inhibits the binding of TBP to the TATA box in vitro and suggested that this was the mechanism of inhibition by TAF II 230.…”

Section: Discussionsupporting

confidence: 82%

“…Results from our experiments indicate this may not the case in our in vivo assay, since overexpression of TAF II 230 did not affect basal or dTBP-enhanced basal CAT expression in the absence of activators. A possible explanation for this finding is that overexpressed TAF II 230 can affect the ability of only native TBP, not TFIID, to bind DNA (35). Since the transfected dTBP assembles into higher-order complexes that probably contain TAFs (Fig.…”

Section: Discussionmentioning

confidence: 98%

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Functional Interaction between p53, the TATA-Binding Protein (TBP), and TBP-Associated Factors In Vivo

Farmer

Colgan

Nakatani

et al. 1996

Molecular and Cellular Biology

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102

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The transcriptional activator p53 is known to interact with components of the general transcription factor TFIID in vitro. To examine the relevance of these associations to transcriptional activation in vivo, plasmids expressing a p53-GAL4 chimera and Drosophila TATA-binding protein (dTBP) were transfected into Drosophila Schneider cells. p53-GAL4 and dTBP displayed a markedly synergistic effect on activated transcription from a GAL4 site-containing reporter that was at least 10-fold greater than observed with other activators tested. A mutant p53 previously shown to be defective in both transcriptional activation in vivo and in binding to TBP-associated factors (TAFs) in vitro, although still capable of binding dTBP, did not cooperate with dTBP, suggesting that TAFs may contribute to this synergy. Providing further support for this possibility, transfected dTBP assembled into rapidly sedimenting complexes and could be immunoprecipitated with anti-TAF antibodies. While overexpression of any of several TAFs did not affect basal transcription, in either the presence or the absence of cotransfected dTBP, overexpression of TAF II 230 inhibited transcriptional activation mediated by p53-GAL4 as well as by GAL4-VP16 and Sp1. Overexpression of TAF II 40 and TAF II 60 also inhibited activation by p53-GAL4 but had negligible effects on activation by GAL4-VP16 and Sp1, while TAF II 110 did not affect any of the activators. TAF-mediated inhibition of activated transcription could be rescued by high levels of exogenous dTBP, which also restored full synergy. These data demonstrate for the first time that functional interactions can occur in vivo between TBP, TAFs, and p53.Exposure to DNA-damaging agents causes cellular levels of the p53 tumor suppressor protein to dramatically increase, resulting in a G 1 /S arrest in the cell cycle. This arrest is presumably due to the direct activation by p53 of genes involved in DNA repair, cell cycle regulation, and apoptosis (for reviews, see references 12 and 23). The role of p53 as a DNA-bindingdependent transcriptional activator is an important one since mutations that alter this ability lead to unregulated cellular growth and tumorigenesis (for a review, see reference 13). Therefore, it is of great interest to understand the mechanism of transcriptional activation by p53.Proper transcriptional activation of class II genes requires specific interactions between activators bound to regulatory elements and the general transcription factors that assemble on the TATA box and/or the initiator element (reviewed in reference 59). Besides TFIID, the factor that directly binds to the TATA box, the general factors include TFIIA, -B, -E, -F, and -H and RNA polymerase II (Pol II) (3, 11, 65), many of which have been shown to interact directly with transcriptional activators in vitro (8,31,40,46,64). The TATA-binding protein (TBP), the TFIID subunit that directly binds the TATA motif (for a review, see reference 26), has also been shown to interact directly with transcriptional activators in vit...

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Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 98%

Functional Interaction between p53, the TATA-Binding Protein (TBP), and TBP-Associated Factors In Vivo

Farmer

Colgan

Nakatani

et al. 1996

Molecular and Cellular Biology

Self Cite

102

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“…Although this region does not have any recognizable motifs, it could be a site for protein-protein interaction. In the TFIID complex, CCG1/TAF II 250 has been shown to interact directly with TBP (Hisatake et al 1993;Ruppert et al 1993), potentially via the N-and C-terminal CCG1/TAF II 250 regions (Kokubo et al 1993), TAF II 55 (Chiang & Roeder 1995), TAF II 30a, TAF II 30b, TAF II 60, TAF II 110, TAF II 150 .…”

Section: Discussionmentioning

confidence: 99%

D‐type cyclin expression is decreased and p21 and p27 CDK inhibitor expression is increased when tsBN462 CCG1/TAF_II250 mutant cells arrest in G1 at the restrictive temperature

et al. 1996

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“…For example, the largest TAF, TAF1, has been reported to be absolutely indispensable for expression of 18% of the mammalian genes (30). TAF1 is known to have kinase activity and acetyltransferase activity (31)(32)(33), but the roles of these activities and the function of TAF1 are still not understood. Although relatively little is known about the functions of any of the TAFs, TFIID structure and composition are thought to be relatively invariant on the assembled PIC.…”

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confidence: 99%

TAF7: A possible transcription initiation check-point regulator

Gégonne

Weissman

Zhou

et al. 2006

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

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Transcription consists of a series of highly regulated steps: assembly of a preinitiation complex (PIC) at the promoter nucleated by TFIID, followed by initiation, elongation, and termination. The present study has focused on the role of the TFIID component, TAF7, in regulating transcription initiation. In TFIID, TAF7 binds to TAF1 and inhibits its intrinsic acetyl transferase activity. We now report that although TAF7 remains bound to TAF1 and associated with TFIID during the formation of the PIC, TAF7 dissociates from the PIC upon transcription initiation. Entry of polymerase II into the assembling PIC is associated with TAF1 and TAF7 phosphorylation, coincident with TAF7 release. We propose that the TFIID composition is dynamic and that TAF7 functions as a check-point regulator suppressing premature transcription initiation until PIC assembly is complete.MHC class I ͉ regulation ͉ preinitiation complex ͉ TFIID I n eukaryotic cells, expression of most protein-encoding genes depends on the RNA polymerase II (Pol II)-dependent transcription machinery. The RNA Pol II machinery assembled on the promoter is composed of distinct complexes that are responsible for effecting the sequential steps of transcription initiation and elongation (1-5). The first step in transcription is the recognition of the core promoter by the TFIID complex and the assembly of a preinitiation complex (PIC) through an ordered recruitment of the general transcription factors (GTFs) TFIIB and TFIIA, followed by the RNA Pol II holoenzyme, the mediator and the remaining GTFs, TFIIF, TFIIE, and TFIIH. Once the PIC has been assembled, transcription initiation ensues: local melting of the promoter DNA, formation of the first phosphodiester bond, followed by the synthesis of a short nascent RNA at which point the polymerase pauses. The initiation of transcription is accompanied by the phosphorylation of serine 5 in the C-terminal domain (CTD) heptad repeat of RNA Pol II (CTD) by the kinase subunit of TFIIH, CDK7 (6-9).Despite the extensive understanding of the general requirements of transcription, many details remain unresolved and there is considerable variation among different promoters and cell types. Promoter recognition is mediated by members of either the TFIID complex family (TFIID, TFIID-like) or the SAGA complex family (e.g., TFTC, PCAF, SAGA) (10-12). In yeast, 90% of gene expression is TFIID-dependent transcription; the remaining 10% is largely dependent on the SAGA complex (13). The TFIID complexes are composed of either the TATAbinding protein (TBP) or a TBP related protein (TRF1, TRF2) and several TBP-associated factors (TAFs) (14-17). The SAGA family complexes do not contain TBP or TBP-related proteins; rather, they contain a GCN5-related histone acetyl transferase (AT) subunit, several adapter and Spt proteins and a subset of TAFs. The composition of the TAFs present in these different complexes varies depending on the structure of the promoter and the cell cycle and tissue-specific gene expression requirement. For example, in yeas...

show abstract

Drosophila 230-kD TFIID subunit, a functional homolog of the human cell cycle gene product, negatively regulates DNA binding of the TATA box-binding subunit of TFIID.

Cited by 94 publications

References 81 publications

Functional Interaction between p53, the TATA-Binding Protein (TBP), and TBP-Associated Factors In Vivo

Functional Interaction between p53, the TATA-Binding Protein (TBP), and TBP-Associated Factors In Vivo

D‐type cyclin expression is decreased and p21 and p27 CDK inhibitor expression is increased when tsBN462 CCG1/TAF_II250 mutant cells arrest in G1 at the restrictive temperature

TAF7: A possible transcription initiation check-point regulator

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Drosophila 230-kD TFIID subunit, a functional homolog of the human cell cycle gene product, negatively regulates DNA binding of the TATA box-binding subunit of TFIID.

Cited by 94 publications

References 81 publications

Functional Interaction between p53, the TATA-Binding Protein (TBP), and TBP-Associated Factors In Vivo

Functional Interaction between p53, the TATA-Binding Protein (TBP), and TBP-Associated Factors In Vivo

D‐type cyclin expression is decreased and p21 and p27 CDK inhibitor expression is increased when tsBN462 CCG1/TAFII250 mutant cells arrest in G1 at the restrictive temperature

TAF7: A possible transcription initiation check-point regulator

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D‐type cyclin expression is decreased and p21 and p27 CDK inhibitor expression is increased when tsBN462 CCG1/TAF_II250 mutant cells arrest in G1 at the restrictive temperature