Specific Interaction of TAFII105 with OCA-B Is Involved in Activation of Octamer-dependent Transcription

Wolstein, Orit; Silkov, Antonina; Revach, Merav; Dikstein, Rivka

doi:10.1074/jbc.275.22.16459

Cited by 23 publications

(25 citation statements)

References 44 publications

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“…The primers used to produce this fragment were 5Ј-GCTTCCGAAATG CCCAGGTG-3Ј and 5Ј-CTCCGGGCCCCGCGATCC-3Ј. The in vitro transcription using the 119-nucleotide U-less reporter was done as described previously (14) Immunodepletion. Purified monoclonal antibodies to DSIF p160 and rabbit polyclonal anti-Oct-2 antibody (5 l each) were incubated with 20 l of protein A/G-Sepharose (Amersham Pharmacia) and 100 l of HEMG buffer for 1 h at 4°C to immobilize the antibodies on the beads.…”

Section: Vol 24 2004 Promoter-mediated Inhibition Of Elongation By mentioning

confidence: 99%

Elongation Inhibition by DRB Sensitivity-Inducing Factor Is Regulated by the A20 Promoter via a Novel Negative Element and NF-κB

Ainbinder

Amir-Zilberstein

Yamaguchi

et al. 2004

Molecular and Cellular Biology

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A20 is an immediate-early NF-B target gene. Prior to NF-B stimulation, the A20 promoter is bound by the polymerase II machinery to allow rapid transcription activation. Here we show that the basal A20 transcription is repressed at the level of elongation in a promoter-specific fashion. Immunodepletion in vitro and RNA interference in cultured cells suggest that the basal elongation inhibition is conferred by DRB sensitivityinducing factor (DSIF). We have identified a negative upstream promoter element called ELIE that controls DSIF activity. Remarkably, following NF-B stimulation, inhibition of the A20 promoter by DSIF persists, but it is now regulated by NF-B rather than ELIE. Similar regulation by DSIF is shown for another NF-Bresponsive gene, the IB␣ gene. These findings reveal an intimate and dynamic relationship between DSIF inhibition of elongation and promoter-bound transcription factors. The potential significance of the differential regulation of DSIF activity by cis-acting elements is discussed.Transcription of mRNA-encoding genes is a multistep process divided into initiation, elongation, and termination. Although regulation of initiation plays a major role in gene expression, it has become apparent that the transcription elongation stage is also critical for regulation of gene expression (for reviews see references 5 and 16). Studies of transcription elongation have revealed the existence of several families of elongation factors governing the activity of polymerase II (Pol II) either positively or negatively. P-TEFb is the bestcharacterized positive elongation factor. It acts to induce Pol II processivity by facilitating the transition from the early to the late and productive elongation phase (for a review, see reference 9). Two negative transcription elongation factors, DRB sensitivity-inducing factor (DSIF) and negative elongation factor (NELF), have recently been identified and characterized. DSIF is composed of two subunits, p160 and p14, which are homologs of the Saccharomyces cerevisiae transcription factors Spt5 and Spt4, respectively (12). NELF is composed of five polypeptides. DSIF and NELF function cooperatively to inhibit RNA Pol II elongation (15).The family of NF-B transcription factors is a central component of the cellular response to a broad range of extracellular signals including inflammatory cytokines, tumor promoters, and chemotherapeutic agents. A major pathway regulating NF-B activity involves its nuclear transport. In unstimulated cells NF-B is retained in the cytoplasm in an inactive form by IB inhibitory proteins. Signals that activate NF-B trigger ubiquitination and degradation of IB, resulting in transport of NF-B into the nucleus (for a recent review see reference 6).The mechanism of rapid transcription activation of NF-Bresponsive genes in vivo and in vitro was recently analyzed (1).Chromatin immunoprecipitation (ChIP) assays showed that induction of NF-B by extracellular signals does not enhance preinitiation complex formation, since general transcription factors, Pol ...

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Section: Vol 24 2004 Promoter-mediated Inhibition Of Elongation By mentioning

confidence: 99%

Elongation Inhibition by DRB Sensitivity-Inducing Factor Is Regulated by the A20 Promoter via a Novel Negative Element and NF-κB

Ainbinder

Amir-Zilberstein

Yamaguchi

et al. 2004

Molecular and Cellular Biology

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“…With the exception of TAF30p (30), all TFIID subunits are encoded by single-copy essential genes, and all display a high degree of sequence conservation among eukaryotes. One of these subunits, yeast TAF130p (also known as TAF145p) (58), and its metazoan counterparts (human and Drosophila TAF250p) contain intrinsic enzymatic activities that contribute to transcription (15,16,47,49,53,54,56).Genetic and biochemical experiments have indicated that direct interactions between the activation domains (AD) of transcriptional activators and the subunits of TFIID play key roles in transactivation (11,22,23,38,40,45,62,63,70,73,74,77). This coactivator function may be manifested at the molecular level by DNA-bound activators either stabilizing (recruiting) TFIID on the TATA box-core promoter (TATA-INR-DPE) (8, 42, 64, 65) of cis-linked genes or, perhaps, by (also) activating latent enzymatic activities residing within the subunits of TFIID itself.…”

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confidence: 99%

Molecular Genetic Dissection of TAF25, an Essential Yeast Gene Encoding a Subunit Shared by TFIID and SAGA Multiprotein Transcription Factors

Kirchner

Sanders

Klebanow

et al. 2001

Molecular and Cellular Biology

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We have performed a systematic structure-function analysis of Saccharomyces cerevisiae TAF25, an evolutionarily conserved, single-copy essential gene which encodes the 206-amino-acid TAF25p protein. TAF25p is an integral subunit of both the 15-subunit general transcription factor TFIID and the multisubunit, chromatinacetylating transcriptional coactivator SAGA. We used hydroxylamine mutagenesis, targeted deletion, alaninescanning mutagenesis, high-copy suppression methods, and two-hybrid screening to dissect TAF25. Temperature-sensitive mutant strains generated were used for coimmunoprecipitation and transcription analyses to define the in vivo functions of TAF25p. The results of these analyses show that TAF25p is comprised of multiple mutable elements which contribute importantly to RNA polymerase II-mediated mRNA gene transcription.mRNA gene transcription is mediated by RNA polymerase II working in concert with multiple general transcription factors (GTFs). The basal mRNA gene transcription machinery, as originally defined in vitro, is comprised of the GTFs TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIIH, which function with RNA polymerase II to promote preinitiation complex (PIC) formation in vitro and in vivo (see references 29 and 55 for reviews). GTFs contribute to PIC formation in multiple ways, either acting sequentially in a stepwise fashion (7) to form a PIC or acting as a single unit comprising the RNA polymerase II holoenzyme (35,39). Although the composition of the basal transcription machinery and its possible modes of action have been fairly well characterized, the mechanisms of transcriptional activation are still poorly understood (44). Transactivator proteins have been shown to interact with a variety of targets, including the protein components of the RNA polymerase II transcription machinery as well as chromatin constituents and activities which modify chromatin. Among these putative transactivator targets are the GTF TFIID and the SAGA (Spt-Ada-Gcn5 acetylase) histone acetyltransferase complex. Both of these multisubunit complexes have been extensively studied in yeasts and metazoans (see references 1, 4, 18, and 66 for recent reviews).Yeast TFIID is composed of 14 TATA box DNA binding protein-associated factors (TAFs) exhibiting molecular masses ranging from 150 to 17 kDa (61). Although the identifies of TFIID subunits are known, the exact stoichiometry of these multiple subunits within the complex is not. With the exception of TAF30p (30), all TFIID subunits are encoded by single-copy essential genes, and all display a high degree of sequence conservation among eukaryotes. One of these subunits, yeast TAF130p (also known as TAF145p) (58), and its metazoan counterparts (human and Drosophila TAF250p) contain intrinsic enzymatic activities that contribute to transcription (15,16,47,49,53,54,56).Genetic and biochemical experiments have indicated that direct interactions between the activation domains (AD) of transcriptional activators and the subunits of TFIID play key roles in transactivation (1...

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“…Conversely, NFAT may rely on recruiting partners that can interact directly with the polymerase complex before it can activate transcription. In the case of NFAT/Oct elements, it is known that OCA-B forms a link between Oct factors and components of the TFIID complex that interacts with the TATA box and RNA polymerase (35,36). In the case of NFAT/AP-1 elements, AP-1 is a strong activator of the TFIID complex.…”

Section: Discussionmentioning

confidence: 99%

Reconstitution of T Cell-Specific Transcription Directed by Composite NFAT/Oct Elements

Bert

Burrows

Hawwari

et al. 2000

The Journal of Immunology

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The complex nature of most promoters and enhancers makes it difficult to identify key determinants of tissue-specific gene expression. Furthermore, most tissue-specific genes are regulated by transcription factors that have expression profiles more widespread than the genes they control. NFAT is an example of a widely expressed transcription factor that contributes to several distinct patterns of cytokine gene expression within the immune system and where its role in directing specificity remains undefined. To investigate distinct combinatorial mechanisms employed by NFAT to regulate tissue-specific transcription, we examined a composite NFAT/AP-1 element from the widely active GM-CSF enhancer and a composite NFAT/Oct element from the T cell-specific IL-3 enhancer. The NFAT/AP-1 element was active in the numerous cell types that express NFAT, but NFAT/Oct enhancer activity was T cell specific even though Oct-1 is ubiquitous. Conversion of the single Oct site in the IL-3 enhancer to an AP-1 enabled activation outside of the T cell lineage. By reconstituting the activities of both the IL-3 enhancer and its NFAT/Oct element in a variety of cell types, we demonstrated that their T cell-specific activation required the lymphoid cofactors NIP45 and OCA-B in addition to NFAT and Oct family proteins. Furthermore, the Oct family protein Brn-2, which cannot recruit OCA-B, repressed NFAT/Oct enhancer activity. Significantly, the two patterns of combinatorial regulation identified in this study mirror the cell-type specificities of the cytokine genes that they govern. We have thus established that simple composite transcription factor binding sites can indeed establish highly specific patterns of gene expression.

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Specific Interaction of TAFII105 with OCA-B Is Involved in Activation of Octamer-dependent Transcription

Cited by 23 publications

References 44 publications

Elongation Inhibition by DRB Sensitivity-Inducing Factor Is Regulated by the A20 Promoter via a Novel Negative Element and NF-κB

Elongation Inhibition by DRB Sensitivity-Inducing Factor Is Regulated by the A20 Promoter via a Novel Negative Element and NF-κB

Molecular Genetic Dissection of TAF25, an Essential Yeast Gene Encoding a Subunit Shared by TFIID and SAGA Multiprotein Transcription Factors

Reconstitution of T Cell-Specific Transcription Directed by Composite NFAT/Oct Elements

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