The progesterone receptor stimulates cell-free transcription by enhancing the formation of a stable preinitiation complex

Klein-Hitpaß, Ludger; Tsai, Sophia Y.; Weigel, Nancy L.; Allan, Grant; Riley, Deborah; Rodríguez, Ronald; Schrader, William T.; Tsai, Ming ler; O’Malley, Bert W.

doi:10.1016/0092-8674(90)90740-6

Cited by 213 publications

(118 citation statements)

References 53 publications

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“…The reporter construct tk-luc, containing the thymidine kinase promoter, is identical to pT81 luc (Nordeen, 1988). The vector ERE,-TATA-luc (kindly provided by L. VaBen) contains two estrogen-responsive elements (Klein-Hitpass et al, 1989) in front of the TATA box from pLovTATA (Klein-Hitpass et al, 1990) driving the luciferase gene.…”

Section: Materials and Methods Expression Vectors And Reporter Constrmentioning

confidence: 99%

Estrogen‐Inducible Derivatives of Hepatocyte Nuclear Factor‐4, Hepatocyte Nuclear Factor‐3 and Liver Factor B1 are Differently Affected by Pure and Partial Antiestrogens

Drewes

Clairmont

Klein-Hitpaß

et al. 1994

European Journal of Biochemistry

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The tissue-specific transcription factors of the hepatocyte nuclear factor-4 (HNF4), hepatocyte nuclear factor-3 (HNF3), and liver factor B1 (LFB1) families are thought to play a role in the development of internal organs and in the tissue-specific expression of many distinct genes. We have now constructed derivatives of these proteins by introducing the hormone-binding domain of the estrogen receptor and show that in transient transfections these chimeric proteins act as estrogeninducible transcription factors with the DNA sequence specificity of the original factors. These chimeric transcription factors are differently affected by the partial estrogen antagonist 4-hydroxytamoxifen and the pure antiestrogen N-n-butyl-ll-(3,17-dihydroxy-estra-l,3,5(1O)-trien-7a-yl)Nmethyl-undecamide (ICI 164384) ; 4-hydroxytamoxifen activates, at least partially, all the chimeric factors and the estrogen receptor, while ICI 164384 surprisingly activates the transcription factors derived from HNF3 and LFBl and inhibits only the estrogen receptor and the HNF4 derivative. Together with the DNA-sequence-binding specificity, the different response to estrogen and antiestrogens makes our estrogen receptor fusion proteins useful tools for the investigation of the roles of HNF4, HNF3 and LFBl in gene expression, differentiation and developmental processes.Over the last decade, the investigation of the mechanisms involved in liver-specific gene expression has led to the identification first of DNA elements responsible for this tissue specificity and subsequently of protein factors which are able to bind specifically to these promoter elements. Many of these factors have recently been cloned and shown to be transcriptional activators of reporter genes containing DNA elements that mediate liver-specific gene expression (Lai and Darnell, 1991;Sladek and Darnell, 1992;Xanthopoulos and Mirkovitch, 1993). According to their DNA-binding specificity, these transcription factors were subdivided into the liver factor B 1 (LFBl), hepatocyte nuclear factor-3 (HNF3), hepatocyte nuclear factor-4 (HNF4), or CCAAT bodenhancerbinding protein (CEBP) families (Xanthopoulos and Mirkovitch, 1993). Using the cloned cDNA and antibodies, it was established that these factors are not restricted to the liver but are also found in other tissues Bartkowski et al., 1993). One approach to understand the role of these tissue-specific transcription factors within a certain cell type and in differentiation and embryogenesis is to introduce these factors into cells in which they are normally not expressed. As it has been shown that estrogen- N-n-butyl-ll-(3,17-dihydroxy-estra-l,3,5(10)-trien-7a-yl)N-methyl-undecamide; LFB1, liver factor B1; VP, viral protein.inducible fusion proteins of transcription factors containing the hormone-binding domain of the estrogen receptor are useful tools to investigate the role of transcription factors in these processes (Umek et al., 1991 ;Burk and Klempnauer, 1991 ;Briegel et al., 1993), we decided to establish estrogendependent deriva...

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Section: Materials and Methods Expression Vectors And Reporter Constrmentioning

confidence: 99%

Estrogen‐Inducible Derivatives of Hepatocyte Nuclear Factor‐4, Hepatocyte Nuclear Factor‐3 and Liver Factor B1 are Differently Affected by Pure and Partial Antiestrogens

Drewes

Clairmont

Klein-Hitpaß

et al. 1994

European Journal of Biochemistry

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“…It should be noted that PR requires ligand to bind DNA in vitro efficiently, which complicates an unambignous assessment of the role of ligand in trans-activation (Bagchi et al 1992). The level of transcription elicited by recombinant PR, glucocorticoid (GR), estrogen (ER), and androgen (AR) was shown to be unaffected by addition of the cognate agonist or antagonist (Klein-Hitpass et al 1990;Tsai et al 1990;Shemschedini et al 1992;Brou et al 1993;De Vos et al 1994}. Ligand effects have been reported for type II receptors. Bacterially expressed TgR~ was shown to repress transcription from the growth hormone gene and other thyroid hormone response element (TRE)-containing promoters in vitro, and this repression could be alleviated by addition of T 3 (Fondell et al 1993).…”

Section: Genes and Developmentmentioning

confidence: 99%

Retinoid-dependent in vitro transcription mediated by the RXR/RAR heterodimer.

Valcárcel

Holz²,

Jiménez³

et al. 1994

Genes Dev.

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The effects of retinoids on gene regulation are mediated by retinoic acid receptors (RARs) and retinoid X receptors (RXRs). Here, we provide the first biochemical evidence that, in vitro, ligand governs the transcriptional activity of RXRa/RARa by inducing conformational changes in the ligand-binding domains. Using limited proteolytic digestion we show that binding of the cognate ligand causes a conformational change in the carboxy-terminal part of the receptor. We also show that recombinant RXRa/RARa is partially active in the absence of exogenously added ligand. Trans-activation depends critically on the ligand-dependent transcriptional activation function AF-2 of RARer. Full activation by recombinant RXRoL/RAR~, however, requires the addition of either all-trans RA, 9-cis RA, or other RAR-specific agonists, whereas an RARa-specific antagonist abolishes trans-activation. Intriguingly, the ligand-dependent AF-2 of RXR does not contribute to the level of transcription from the RARI32 promoter in vitro even when the cognate ligand (9-cis RA1 is bound. Thus, the major role of RXR in trans-activation of the RARI32 promoter is to serve as an auxiliary factor required for the binding of RAR which, in turn, is directly responsible for transcriptional activity.

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“…As controls, 6 g of nuclear proteins were prepared from Sf9 cells infected with baculovirus expressing either mRXR␤ (positive control, lane 1) or wildtype virus lacking RXR (wt, negative control, lane 2) and probed with 32 P-labeled GST-RXR. Labeled GST-RXR (but not labeled GST-0, lanes 6 -8) detected a band in bacterial extracts containing human TFIIB (lanes [3][4][5]. that 32 P-labeled GST-RXR detected TR, but only if the C terminus of the labeled RXR molecule was intact.…”

Section: Fig 1 Interaction Between Rxr and Tfiib Is Directmentioning

confidence: 99%

“…␤-Galactosidase activity (from the lacZ gene) of at least six independent yeast colonies grown in the absence (open bar) or presence of 1 M 9-cis-RA (black bar), normalized for protein, is shown in relative light units (mean Ϯ S.E.). Lower panels, immunoblot analysis of representative yeast extracts functionally analyzed (in lanes [1][2][3][4][5][6] were probed with a mouse monoclonal anti-RXR␤ (40) antibody 13.17 (anti-RXR) or a rabbit polyclonal antibody directed against amino acids 299 -316 of TFIIB (anti-TFIIB; Santa Cruz Biotechnology, Santa Cruz, CA) and incubated with secondary antibody (anti-mouse Ig or anti-rabbit Ig, peroxidase-linked antibody, respectively). Protein-antibody complexes were detected by enhanced chemiluminescence (ECL, Amersham Corp., UK) and exposed to autoradiography.…”

Section: Fig 1 Interaction Between Rxr and Tfiib Is Directmentioning

confidence: 99%

“…1-3 and references therein). Ligand binding to nuclear hormone receptors leads to assembly of a functional preinitiation complex (PIC) 1 and subsequent RNA transcription in vitro (4,5). Activated transcription of RNA polymerase II (RNAPII) genes requires binding of transcription factor IID (TFIID) to the TATA element, which is facilitated by TFIIA, and stepwise assembly of the following transcription factors: TFIIB, RNAPII/TFIIF, TFIIE, and TFIIH (reviewed in Refs.…”

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confidence: 99%

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Interaction between the Retinoid X Receptor and Transcription Factor IIB Is Ligand-dependent in Vivo

Leong

Wang

Marton

et al. 1998

Journal of Biological Chemistry

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The retinoid X receptor (RXR) influences gene activation through heterodimeric and homodimeric association with DNA and associates with TATA binding protein, TAF110, and cAMP response element-binding protein-binding protein; yet the molecular mechanisms responsible for gene activation by RXRs remain incompletely defined. Since the general transcription factor IIB (TFIIB) is a common target of sequence-specific transcriptional activators, we suspected that RXR might regulate target genes via an interaction with TFIIB. Coimmunoprecipitation, far Western analysis, and glutathione S-transferase binding studies indicated that murine RXR␤ (mRXR␤) was capable of binding to human TFIIB in vitro. Functional analysis with a dual-hybrid yeast system and cotransfection assays revealed the interaction of mRXR␤ with TFIIB to be ligand-dependent in vivo. Truncation experiments mapped the essential binding regions to the carboxyl region of mRXR␤ (amino acids (aa) 254 -389) and two regions in the carboxyl region of TFIIB (aa 178 -201 and aa 238 -271). Furthermore, the ⌬390 -410 mRXR␤ mutant bound to TFIIB in vitro but was not active in the dual-hybrid yeast system, suggesting that the extreme carboxyl region of RXR was required for in vivo interaction with TFIIB. These data indicate that interaction of mRXR␤ with TFIIB is specific, direct, and ligand-dependent in vivo and suggest that gene activation by RXR involves TFIIB.Nuclear hormone receptors are ligand-dependent transcription factors that regulate numerous cellular functions, including growth, development, differentiation, reproduction, and metabolism (Refs. 1-3 and references therein). Ligand binding to nuclear hormone receptors leads to assembly of a functional preinitiation complex (PIC) 1 and subsequent RNA transcription in vitro (4, 5). Activated transcription of RNA polymerase II (RNAPII) genes requires binding of transcription factor IID (TFIID) to the TATA element, which is facilitated by TFIIA, and stepwise assembly of the following transcription factors: TFIIB, RNAPII/TFIIF, TFIIE, and TFIIH (reviewed in Refs. 6 and 7). TFIID includes the TATA binding protein (TBP) associated factors (TAFs) (Ref.7, and references therein). Interaction of nuclear receptors with the basal transcription complex may occur directly (8 -14) or in association with TAFs (15) or other cofactors (Refs. 16 -25; reviewed in Refs. 26 and 27). Ligand binding to the receptor results in recruitment of factors that facilitate assembly of an activated complex (28 -30) or, conversely, the release of repressor molecules, such as SMRT (16) or N-CoR (17, 18) that inhibit transcription (16 -18, 31-32). A significant advance was the demonstration that TFIIB interacts with the estrogen receptor (10), progesterone receptor (10), chicken ovalbumin upstream promoter-transcription factor (10), thyroid hormone receptor (TR) (11, 31), and vitamin D receptor (VDR) (12)(13)(14). The interaction of nuclear hormone receptors with TFIIB is significant since recruitment of TFIIB to the PIC by transcriptional activat...

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The progesterone receptor stimulates cell-free transcription by enhancing the formation of a stable preinitiation complex

Cited by 213 publications

References 53 publications

Estrogen‐Inducible Derivatives of Hepatocyte Nuclear Factor‐4, Hepatocyte Nuclear Factor‐3 and Liver Factor B1 are Differently Affected by Pure and Partial Antiestrogens

Estrogen‐Inducible Derivatives of Hepatocyte Nuclear Factor‐4, Hepatocyte Nuclear Factor‐3 and Liver Factor B1 are Differently Affected by Pure and Partial Antiestrogens

Retinoid-dependent in vitro transcription mediated by the RXR/RAR heterodimer.

Interaction between the Retinoid X Receptor and Transcription Factor IIB Is Ligand-dependent in Vivo

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