A functional interaction between ATF7 and TAF12 that is modulated by TAF4

Hamard, Pierre-Jacques; Dalbiès-Tran, Rozenn; Hauss, Charlotte; Davidson, Irwin; Kédinger, Claude; Chatton, Bruno

doi:10.1038/sj.onc.1208565

Cited by 25 publications

(46 citation statements)

References 60 publications

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“…N-terminal Taf12p sequences have been shown by others to contribute to transcrip- VOL. 27,2007 TFIID-Rap1p INTERACTION 307 tional readout in several other in vivo contexts (27,56,96). In addition to the tight binding of Rap1p to Taf12p, we reproducibly detect somewhat lower-affinity binding of Rap1p to Taf4p and Taf5p.…”

Section: Discussionmentioning

confidence: 70%

Yeast TFIID Serves as a Coactivator for Rap1p by Direct Protein-Protein Interaction

Garbett

Tripathi

Cencki

et al. 2007

Molecular and Cellular Biology

127

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In vivo studies have previously shown that Saccharomyces cerevisiae ribosomal protein (RP) gene expression is controlled by the transcription factor repressor activator protein 1 (Rap1p) in a TFIID-dependent fashion. Here we have tested the hypothesis that yeast TFIID serves as a coactivator for RP gene transcription by directly interacting with Rap1p. We have found that purified recombinant Rap1p specifically interacts with purified TFIID in pull-down assays, and we have mapped the domains of Rap1p and subunits of TFIID responsible. In vitro transcription of a UAS RAP1 enhancer-driven reporter gene requires both Rap1p and TFIID and is independent of the Fhl1p-Ifh1p coregulator. UAS RAP1 enhancer-driven transactivation in extracts depleted of both Rap1p and TFIID is efficiently rescued by addition of physiological amounts of these two purified factors but not TATA-binding protein. We conclude that Rap1p and TFIID directly interact and that this interaction contributes importantly to RP gene transcription.Eukaryotic mRNA gene transcription is controlled by the action of modular enhancer-binding transactivators, proteins composed of separable DNA binding domains (DBD) and activation domains (AD). DNA-bound transactivators functionally interact with the mRNA gene transcription machinery, the so-called general transcription factors (GTFs) TFIIA, -B, -D, -E, -F, and -H plus RNA polymerase II (RNAP II), to stimulate formation and/or function of the RNAP II preinitiation complex (PIC) (67). Activators also collaborate with one or more factors termed coactivators, proteins that serve as receptors for the transfactor-AD activation signal. Coactivators link transactivator-enhancer DNA binding to the PIC (43) and can be divided into several classes: those that are chromatin active, the mediator complex, and the individual components of the mRNA gene transcription machinery itself.One of the first and likely rate-limiting steps in mRNA gene transcription is the binding of TFIID to the promoter (36,40,47). TFIID is a multisubunit assembly composed of 15 evolutionarily conserved (86) subunits, the TATA-binding protein (TBP) and 14 TBP-associated factors (TAFs) (72). This GTF displays high-affinity, sequence-specific promoter DNA binding activity. Two classes of yeast mRNA-encoding genes have been defined with respect to TFIID TAF function; the first, which is TAF dependent (TAF dep ), requires TAF function for transcription, while the second and smaller group is TAF independent (TAF ind ) (29,31,45,58,81,92). Both types of genes require TBP for wild-type (WT) levels of transcription, but in the case of the TAF ind genes, TBP appears to be recruited via mechanisms distinct from TFIID (4, 80).When mRNA-encoding genes are monitored for TBP and TAF occupancy by chromatin immunoprecipitation (ChIP) assay, TAF dep genes exhibit higher TAF/TBP occupancy ratios than TAF ind genes (39, 45). Three models for TAF function have been proposed (22, 23): TAFs mediate core promoter recognition; TAFs provide essential catalytic activities tha...

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Section: Discussionmentioning

confidence: 70%

Yeast TFIID Serves as a Coactivator for Rap1p by Direct Protein-Protein Interaction

Garbett

Tripathi

Cencki

et al. 2007

Molecular and Cellular Biology

127

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“…Interestingly, TAF12, which heterodimerizes with TAF4 or TAF4b, has also been shown to directly interact with AP-1 family member ATF7, controlling transcription (40). In the present study, we suggest that TAF4b functions as a coactivator of integrin α6 transcription in concert with activator c-Jun or, depending on the cell type, with other AP-1 family members.…”

Section: Discussionmentioning

confidence: 57%

TAF4b and Jun/Activating Protein-1 Collaborate to Regulate the Expression of Integrin α6 and Cancer Cell Migration Properties

Kalogeropoulou

Voulgari

Kostourou

et al. 2010

Molecular Cancer Research

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The TAF4b subunit of the transcription factor IID, which has a central role in transcription by polymerase II, is involved in promoter recognition by selective recruitment of activators. The activating protein-1 (AP-1) family members participate in oncogenic transformation via gene regulation. Utilizing immunoprecipitation of endogenous protein complexes, we documented specific interactions between Jun family members and TATA box binding protein-associated factors (TAF) in colon HT29 adenocarcinoma cells. Particularly, TAF4b and c-Jun were found to colocalize and interact in the nucleus of advanced carcinoma cells and in cells with epithelial-tomesenchymal transition (EMT) characteristics. TAF4b was found to specifically regulate the AP-1 target gene involved in EMT integrin α6, thus altering related cellular properties such as migration potential. Using a chromatin immunoprecipitation approach in colon adenocarcinoma cell lines, we further identified a synergistic role for TAF4b and c-Jun and other AP-1 family members on the promoter of integrin α6, underlining the existence of a specific mechanism related to gene expression control. We show evidence for the first time of an interdependence of TAF4b and AP-1 family members in cell type-specific promoter recognition and initiation of transcription in the context of cancer progression and EMT. Mol Cancer Res; 8(4); 554-68. ©2010 AACR.

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“…In vitro pull-down assays were used to determine whether EKLF interacts with any of the TAFs that contain a histone fold domain (HFD). These TAFs (TAF4, TAF12, TAF6, and TAF9) have been implicated in interactions with other activators and in being recruited to promoters (29)(30)(31)(32)(33). We find that full-length EKLF only interacts with TAF9 ( Fig.…”

Section: Resultsmentioning

confidence: 67%

Distinct modes of gene regulation by a cell-specific transcriptional activator

Sengupta

Cohet

Morlé

et al. 2009

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

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The architectural layout of a eukaryotic RNA polymerase II core promoter plays a role in general transcriptional activation. However, its role in tissue-specific expression is not known. For example, differing modes of its recognition by general transcription machinery can provide an additional layer of control within which a single tissue-restricted transcription factor may operate. Erythroid Kruppel-like factor (EKLF) is a hematopoietic-specific transcription factor that is critical for the activation of subset of erythroid genes. We find that EKLF interacts with TATA binding protein-associated factor 9 (TAF9), which leads to important consequences for expression of adult ␤-globin. First, TAF9 functionally supports EKLF activity by enhancing its ability to activate the ␤-globin gene. Second, TAF9 interacts with a conserved ␤-globin downstream promoter element, and ablation of this interaction by ␤-thalassemia-causing mutations decreases its promoter activity and disables superactivation. Third, depletion of EKLF prevents recruitment of TAF9 to the ␤-globin promoter, whereas depletion of TAF9 drastically impairs ␤-promoter activity. However, a TAF9-independent mode of EKLF transcriptional activation is exhibited by the ␣-hemoglobin-stabilizing protein (AHSP) gene, which does not contain a discernable downstream promoter element. In this case, TAF9 does not enhance EKLF activity and depletion of TAF9 has no effect on AHSP promoter activation. These studies demonstrate that EKLF directs different modes of tissue-specific transcriptional activation depending on the architecture of its target core promoter.

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A functional interaction between ATF7 and TAF12 that is modulated by TAF4

Cited by 25 publications

References 60 publications

Yeast TFIID Serves as a Coactivator for Rap1p by Direct Protein-Protein Interaction

Yeast TFIID Serves as a Coactivator for Rap1p by Direct Protein-Protein Interaction

TAF4b and Jun/Activating Protein-1 Collaborate to Regulate the Expression of Integrin α6 and Cancer Cell Migration Properties

Distinct modes of gene regulation by a cell-specific transcriptional activator

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