Nuclear acceptor sites for sex steroid hormone receptors in chromatin

Spelsberg, T. C.; Goldberger, Amy; Horton, Michael; Hora, J.

doi:10.1016/0022-4731(87)90304-9

Cited by 12 publications

(7 citation statements)

References 52 publications

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“…Early characterization of the chromatin acceptor sites has been reported for the progesterone (P) [Spelsberg et al, 1983[Spelsberg et al, , 1984[Spelsberg et al, , 1987aPerry and Lopez, 1978;Lopez et al, 1985;Cobb and Leavitt, 19871, estrogen (E,) [Ruh et al, 1981;Ross and Ruh, 1984;Singh et al, 19841, and androgen [Mainwaring et al, 1976;Klyzsejko-Stefanowicz et al, 1976;Wang, 1978;Rennie et al, 19871 receptors in a variety of animal systems. Chromatin acceptor sites for the avian oviduct progesterone receptor (PR) have been studied extensively and found to consist of complexes of specific acceptor proteins tightly bound t o specific DNA sequences [Spelsberg et al, 1972[Spelsberg et al, , 1984[Spelsberg et al, , 1987a[Spelsberg et al, ,b, 1988Schuchard et al, 1991a,b;Pikler et al, 1976;Kon and Spelsberg, 1982;Hora et al, 1986;Goldberger et al, 1987;Goldberger and Spelsberg, 1988;Rejman et al, 19911.…”

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confidence: 96%

Immunohistochemical localization of the avian progesterone receptor and its candidate receptor binding factor (RBF‐1)

Zhuang

Landers

Schuchard

et al. 1993

J of Cellular Biochemistry

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An avian oviduct nuclear matrix protein in the 6-10 kDa size range has been implicated to function in the cell-free nuclear binding of the avian oviduct progesterone receptor (PR). This protein, termed the receptor binding factor-1 (RBF-1), has been purified and partially characterized [Schuchard et al.: Biochemistry 30:4535-4542, 1991]. This paper describes the immunohistochemical co-localization of the RBF-1 and PR in the avian oviduct cell nuclei and rat reproductive cell nuclei using antibodies directed specifically against the RBF-1 and activated PR. In the undifferentiated oviduct, the immunoreactivities for both PR and RBF-1 were co-localized in the nuclei of only epithelial cells, but not the stromal cells or smooth muscle cells. In the partially differentiated oviduct of estrogen treated chicks, the immunoreactivity co-localized in the nuclei of not only epithelial but also glandular and stromal cells. Staining for the PR, but not RBF-1, was detected in the smooth muscle cells. The intensity of the PR but not the RBF-1 staining was markedly down-regulated in these cells at 2 and 6 h after treatment of the animals with progesterone (P). However, the band patterns for RBF-1 in the Western blots did show qualitative changes which may reflect P-induced posttranslational modifications which alter the epitope on the RBF-1. Interestingly, immunohistochemical analysis of several reproductive tissues of the rat showed that certain cell types in the uterus, ovary, and prostate displayed strong positive nuclear staining for an RBF-1-like antigen(s).(ABSTRACT TRUNCATED AT 250 WORDS)

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confidence: 96%

Immunohistochemical localization of the avian progesterone receptor and its candidate receptor binding factor (RBF‐1)

Zhuang

Landers

Schuchard

et al. 1993

J of Cellular Biochemistry

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“…Briefly, purified RBF was solubilized in 6 M guanidine-HCl in reconstitution buffer (10 mM Tris, 1 mM EDTA, 1 mM dithiothreitol, 0.2 mM PMSF) to a concentration of 250 ng/ml. This concentration of the RBF was found to be important for optimal protein renaturation and reconstitution of PR-binding sites on the DNA (26,30,48). It was also found in these current studies to be important for achieving the optimal DNA sequence-specific binding.…”

Section: Isolation and Purification Of Rbf By Preparativementioning

confidence: 57%

“…In our laboratory, a specific "acceptor protein," RBF, was isolated based on its ability to generate saturable, high affinity binding sites on avian and mammalian genomic DNAs and characterized as a component of the chromatin nuclear matrix acceptor sites for the avian oviduct PR (22,23,25,26,29,30,67,68). The RBF failed to generate these sites when using insect and prokaryotic genomic DNA.…”

Section: Discussionmentioning

confidence: 99%

“…2 Earlier studies had indicated that specific DNA sequences were important when generating RBF/PR-binding sites. The PR-binding sites could only be generated when the purified RBF was bound to mammalian genomic DNA, but not when the RBF was complexed to prokaryotic, or lower eukaryotic genomic DNAs (29,30). The PR-binding sites could also be generated with the genomic sequences of the c-myc gene but not those of the ovalbumin gene (31).…”

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confidence: 98%

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A DNA-binding Element for a Steroid Receptor-binding Factor Is Flanked by Dual Nuclear Matrix DNA Attachment Sites in the c-myc Gene Promoter

Lauber

Barrett

Subramaniam

et al. 1997

Journal of Biological Chemistry

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The receptor-binding factor (RBF) for the avian oviduct progesterone (Pg) receptor (PR) has previously been shown to be a unique 10-kDa nuclear matrix protein that generates high affinity PR-binding sites on avian DNA. This paper describes the use of Southwestern blot and DNA gel shift analyses with RBF protein to identify a minimal 54-base pair RBF-binding element in the matrix-associated region (MAR) of the Pg-regulated c-myc gene promoter. This element contains a 5 -GC-rich domain and a 3 -AT-rich domain, the latter of which has a homopurine/homopyrimidine structure. The gel shift assays required the generation of an RBF-maltose fusion protein (RBF-MBP), which specifically binds this element and is supershifted when the anti-RBF polyclonal antibody is added. Computer analysis of the fulllength amino acid sequence for RBF predicts a DNAbinding motif involving a ␤-sheet structure at the N-terminal domain. Southern blot analyses using nuclear matrix DNA suggests that there are dual MAR sites in the c-myc promoter, which flank an intervening domain containing the RBF element. The co-transfection of this MAR sequence, containing the RBF element and cloned into a luciferase reporter vector, together with an RBF expression vector construct, into steroid treated human MCF-7 cells, results in a decrease of the c-myc promoter activity relative to control transfections containing only the parent vector of the RBF expression construct. These data suggest that a unique chromatin/ nuclear matrix structure, composed of the RBF-DNA element complex which is flanked by nuclear matrix attachment sites, serves to bind the PR and repress the c-myc promoter.The classic model of steroid hormone action suggests that ligand-bound receptors dimerize and bind to specific sites (acceptor sites) on the chromatin/DNA to alter gene expression. In many genes, the steroid receptors (SR) 1 bind to specific cisacting DNA sequences, referred to as hormone response elements (for reviews, see Refs. 1-3). These elements function as enhancer-like DNA sequences and are required for the steroid hormone regulation of transcription. However, not all steroidresponsive genes contain these elements, and several other pathways and participating nuclear proteins have now been identified. The SR regulation of gene transcription has now been shown to involve 1) interactions of the SR with transcription factors, such as the AP-1 complex (for review, see Refs. 2-4); 2) interactions of SR with accessory factors, which appear to function by assisting the binding of the receptor to the steroid response elements, or to transcription factors (for reviews see Refs. 4 -6 and references therein); and finally, 3) interactions of SR with specific chromatin structures including the nuclear matrix (see Refs. 7-15 and references therein). In the latter, a class of high affinity binding sites (acceptor sites) for SRs in the nuclei, chromatin, and nuclear matrix DNAbinding proteins (e.g. acceptor proteins) has been reported by many laboratories for most of the steroid hormone...

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“…The amino terminus of the progesterone receptor has been shown to help select the target gene, and a synthetic receptor construct was shown to retain selectively one but not another effect (33). Some steroid receptor target genes have variable numbers of receptor recognition elements, thereby presenting opportunities for varying cooperative effects in receptor actions (2,4,6). Heterogeneous coupling mechanisms are also possible through receptor interactions with an increasing spectrum of transcription factors (34,35).…”

Section: Introductionmentioning

confidence: 99%

Selective expression of a normal action of the 1,25-dihydroxyvitamin D3 receptor in human skin fibroblasts with hereditary severe defects in multiple actions of that receptor.

Bársony¹,

McKoy²,

DeGrange³

et al. 1989

J. Clin. Invest.

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We evaluated three actions of 1,25-dihydroxycholecalciferol 11,25-(OH)2D31 in human skin fibroblasts to test for heterogeneity in hormone-response coupling. In fibroblasts from normal subjects the 1,25-OH)2D3 concentrations for half-maximal effect (EC50) were: for mitogenic effect 0.0001-0.0005 nM, for antimitogenic effect 1 nM, and for induction of 25-OHD3 24-hydroxylase (24-OHase) 5 nM. To evaluate the effects of mutations presumed to be in the gene for the 1,25-(OH)2D3 receptor we examined cell lines representing four kindreds with hereditary resistance to 1,25-(OH)2D3 ("mutant" cell lines). In one mutant cell line all three 1,25-(OH)2D3 actions were severely abnormal. In one mutant cell line 24-OHase induction and mitogenic action were undetectable, but EC50 and maximal effect were normal for antimitogenic action of 1,25-(OH1)D3. In two mutant cell lines 24-OHase induction and antimitogenic actions were undetectable or severely impaired but mitogenic action was normal in EC50 and normal or increased in maximal effect. The mitogenic and antimitogenic actions in normal cells showed a similar profile of potency ratios for 1,25-(OH)2D3 and six analogues. Whenever a mutant cell showed a normal or even an abnormal mitogenic or antimitogenic effect of 1,254-OH)2D3, these effects showed potency ratios similar to wild type, suggesting mediation by a similar 1,2540H)2D3 receptor.We conclude that three 1,25-(OHhD3 actions show important differences in hormone response coupling indicated by differences in EC50 for 1,25-(OH)2D3 and by different consequences of receptor mutations.

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Nuclear acceptor sites for sex steroid hormone receptors in chromatin

Cited by 12 publications

References 52 publications

Immunohistochemical localization of the avian progesterone receptor and its candidate receptor binding factor (RBF‐1)

Immunohistochemical localization of the avian progesterone receptor and its candidate receptor binding factor (RBF‐1)

A DNA-binding Element for a Steroid Receptor-binding Factor Is Flanked by Dual Nuclear Matrix DNA Attachment Sites in the c-myc Gene Promoter

Selective expression of a normal action of the 1,25-dihydroxyvitamin D3 receptor in human skin fibroblasts with hereditary severe defects in multiple actions of that receptor.

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