Sequence-specific DNA binding of the progesterone receptor to the uteroglobin gene: effects of hormone, antihormone and receptor phosphorylation.

Bailly, Alain; Page, Charlotte; Rauch, Michel; Milgröm, Edwin

doi:10.1002/j.1460-2075.1986.tb04634.x

Cited by 186 publications

(71 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…BIOL. progesterone receptor on other genes (1,14,29). On the VTG II gene fragment, the DNase I-hypersensitive sites were localized at positions -620 and -612 to -615 on the lower DNA strand (Fig.…”

Section: Resultsmentioning

confidence: 95%

“…In vitro receptor-DNA binding studies have shown that this hexanucleotide and neighboring sequences on the VTG II gene are bound by the glucocorticoid receptor (26) and could also possibly be recognized by the androgen receptor (6). The hexanucleotide motif is also part of the recognition sequence of the progesterone receptor (1,14,29).The close proximity of the hexanucleotide motif to the ERED on the VTG II gene prompted us to study the functional interaction of these two elements with progestin, androgens, and estradiol in transfection experiments in T47D cells that contain receptors for all three steroid hormones (6). In this communication we present the results of these studies.…”

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Estrogen and progesterone receptor-binding sites on the chicken vitellogenin II gene: synergism of steroid hormone action.

Cato¹,

Heitlinger²,

Ponta³

et al. 1988

Mol. Cell. Biol.

View full text Add to dashboard Cite

The chicken vitellogenin II gene is transcriptionally activated by estrogens. In transient transfection experiments in human T47D cells that contain receptors for various steroids, we showed estradiol, progestin, and androgen responses of a chimeric chicken vitellogenin II construct. This construct consists of DNA sequences from -626 to -590 upstream of the start of transcription of the chicken viteliogenin gene linked to the herpes simplex virus thymidine kinase promoter driving the transcription of the bacterial chloramphenicol acetyltransferase gene. Treatment of the transfected T47D cells with a combination of estradiol and the progestin R5020 led to a superinduction of chloramphenicol acetyltransferase activity, showing a synergistic action of these two steroids. This synergism was not observed upon treatment of the transfected cells with estradiol and the androgen dihydrotestosterone. Using point mutations in the vitellogenin gene fragment, we showed in functional and in in vitro DNase I footprinting assays with a purified progesterone receptor that, for the synergistic action of estradiol and R5020 to occur, the progesterone receptor must be bound to the vitellogenin gene fragment. The progesterone receptor-binding site was localized at -610 to -590, close to the consensus sequence (-626 to -613) for estrogen receptor binding and function. We therefore demonstrate here that two different steroid hormones can be functionally synergistic through the interaction of their corresponding receptors with two different binding sites adjacent to one another.The regulation of gene expression by steroid hormones is thought to occur through the interaction of steroid hormone receptor complexes with discrete nucleotide sequences in the neighborhood of the promoters of inducible genes (for reviews, see references 2 and 35). Short perfect or imperfect palindromic sequences that mediate steroid hormone action have been identified near the promoters of a number of steroid hormone-regulated genes. For example, 13-base-pair (bp) palindromic elements that mediate the estrogen response have been identified near the promoters of the Xenopus and chicken vitellogenin genes (4,17,18,19,22). Similarly, 15-bp perfect or imperfect palindromes that encompass the hexanucleotide motif 5'-TGTT/CCT-3' have been shown to mediate glucocorticoid and progestin responses in a number of genes (5,6,29,30). The delimitation of these short nucleotide sequences was achieved through gene transfer studies with either in vitro mutagenesis of known hormone receptor-binding sites (6) or different chimeras containing synthetic oligonucleotides (13,17,30). In a number of hormone response elements, such as that in mouse mammary tumor virus DNA (3, 6), the tyrosine aminotransferase gene (13), and the Xenopus vitellogenin Bi and chicken vitellogenin II (VTG II) genes (4,16,22,27) sites function by cooperating with the binding sites for other transcriptional factors that lie in their immediate vicinity.In the VTG II gene, a gene whose transcription is known t...

show abstract

Section: Resultsmentioning

confidence: 95%

mentioning

confidence: 99%

See 1 more Smart Citation

Estrogen and progesterone receptor-binding sites on the chicken vitellogenin II gene: synergism of steroid hormone action.

Cato¹,

Heitlinger²,

Ponta³

et al. 1988

Mol. Cell. Biol.

View full text Add to dashboard Cite

show abstract

“…The glucocorticoid and progesterone receptors bind to similar sequences within these fragments, suggesting that the binding sites may be closely related, but distinct (5, 6). Both types of receptors also bind to partially overlapping sequences in the rabbit uteroglobin gene (7,8). These sequences, however, have not been functionally characterized.…”

Section: Introductionmentioning

confidence: 99%

A DNA sequence of 15 base pairs is sufficient to mediate both glucocorticoid and progesterone induction of gene expression.

Strähle

Klöck

Schütz

1987

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

311

126

View full text Add to dashboard Cite

To defmie the recognition sequence of the glucocorticoid receptor and its relationship with that of the progesterone receptor, oligonucleotides derived from the glucocorticoid response element of the tyrosine aminotransferase gene were tested upstream of a heterologous promoter for their capacity to mediate effects of these two steroids. We show that a 15-base-pair sequence with partial symmetry is sufficient to confer glucocorticoid inducibility on the promoter of the herpes simplex virus thymidine kinase gene. The same 15-base-pair sequence mediates induction by progesterone. Point mutations in the recognition sequence affect inducibility by glucocorticoids and progesterone similarly. Together with the strong conservation of the sequence of the DNA-binding domain of the two receptors, these data suggest that both proteins recognize a sequence that is similar, if not the same.The effect of steroid hormones on specific gene transcription is mediated by receptors to which the hormones bind with high selectivity and affinity. Activation of transcription results from binding of the hormone-receptor complex to specific sequences of inducible genes (1, 2). Surprisingly, it has been observed that fragments of the chicken lysozyme gene and of the long terminal repeat of mouse mammary tumor virus that confer glucocorticoid inducibility also allow progesterone induction (3, 4). The glucocorticoid and progesterone receptors bind to similar sequences within these fragments, suggesting that the binding sites may be closely related, but distinct (5, 6). Both types of receptors also bind to partially overlapping sequences in the rabbit uteroglobin gene (7,8). These sequences, however, have not been functionally characterized. To define the sequence requirements for specific binding of the glucocorticoid receptor and to determine the degree to which this sequence overlaps with the recognition sequence for the progesterone receptor, a minimal glucocorticoid response element (GRE) 15 base pairs (bp) in length was defined. This 15-bp sequence is part of the GRE region of the tyrosine aminotransferase (TAT) gene protected against DNase I digestion by the purified glucocorticoid receptor (9). We demonstrate here that the same 15-mer which confers responsiveness to glucocorticoids also mediates progesterone induction. Since point mutations in this 15-bp sequence affect inducibility by both steroids similarly, we suggest that the recognition sequences of the glucocorticoid and progesterone receptors are similar, if not identical. MATERIALS AND METHODSPlasmid Constructions. Oligonucleotides were prepared with an Applied Biosystems 380A DNA synthesizer and purified as recommended by the manufacturer. Annealing of the complementary strands, which generated BamHI or Xba I cohesive ends, and cloning upstream of the herpes simplex virus thymidine kinase (TK) promoter in pBLCAT2 (10) were done by standard procedures (11). pBLCAT2 contains the complete TK promoter (-105 to +62) linked to the chloramphenicol acetyltransferase (CAT) co...

show abstract

“…The potential cis-acting elements for progesterone activation of the gene have only been mapped in DNA binding experiments in vitro. Progesterone receptor-binding sites have been assigned to the first intron of the gene (15), as well as to a region between 2.4 and 2.7 kb upstream of the transcription start site, where two clusters of three imperfect binding sites for glucocorticoid and progesterone receptors have been found (16,17). The relevance of these upstream receptor-binding sites was supported by the appearance of adjacent progesterone inducible DNase I-hypersensitive sites in chromatin of isolated nuclei from endometrial epithelium (17).…”

mentioning

confidence: 99%

Hormone-dependent Recruitment of NF-Y to the Uteroglobin Gene Enhancer Associated with Chromatin Remodeling in Rabbit Endometrial Epithelium

Scholz

Truss

Beato

1999

Journal of Biological Chemistry

View full text Add to dashboard Cite

Expression of the rabbit uteroglobin gene is hormonally induced in cells of the endometrial epithelium during the preimplantation phase of pregnancy. Here we show that progesterone activation of the gene is mediated by two clusters of hormone responsive elements located between 2.4 and 2.7 kilobase pairs upstream of the transcriptional start site. Between these two clusters, genomic footprinting studies in the intact endometrial epithelium reveal the hormone-inducible occupancy of several cis-acting elements. One of the protected elements shows sequence homology to the consensus binding site of the transcription factor NF-Y, which binds to the element in gel shift experiments. This uteroglobin Y box is essential for enhancer activity in transient transfection experiments with endometrial and non-endometrial cell lines, in accordance with the ubiquitous expression of NF-Y. To understand why binding of this ubiquitous factor to the uteroglobin Y box in endometrium depends on hormone induction, we examined the chromatin structure of the relevant gene region. In the uninduced state, the enhancer region appears to be organized into positioned nucleosomes. Upon hormone induction, this nucleosomal pattern is lost and the enhancer region becomes hypersensitive to nucleases, suggesting that a hormone-induced change in the local chromatin structure unmasks previously unaccessible binding sites for transcription factors. Our results emphasize the limitations of using transient transfection assays for the functional analysis of cis-acting elements and underline the need for including the native chromatin organization in this kind of studies.

show abstract

Sequence-specific DNA binding of the progesterone receptor to the uteroglobin gene: effects of hormone, antihormone and receptor phosphorylation.

Cited by 186 publications

References 38 publications

Estrogen and progesterone receptor-binding sites on the chicken vitellogenin II gene: synergism of steroid hormone action.

Estrogen and progesterone receptor-binding sites on the chicken vitellogenin II gene: synergism of steroid hormone action.

A DNA sequence of 15 base pairs is sufficient to mediate both glucocorticoid and progesterone induction of gene expression.

Hormone-dependent Recruitment of NF-Y to the Uteroglobin Gene Enhancer Associated with Chromatin Remodeling in Rabbit Endometrial Epithelium

Contact Info

Product

Resources

About