Effects of RNA and ribonuclease on the binding of estrogen and glucocorticoid receptors from MCF-7 cells to DNA-cellulose.

Chong, Ming Ta; Lippman, Marc E.

doi:10.1016/s0021-9258(19)81063-3

Cited by 90 publications

(6 citation statements)

References 17 publications

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“…More than two decades ago, RNAs, such as tRNAs and synthetic polyribonucleotides, were reported to bind steroid receptors, preventing these receptors from binding their target DNA sequences (22,46,47). RNA purified from White Leghorn chicks and MCF-7 cells inhibited the association of the vitamin D receptor, the estrogen receptor, and the GR with their respective DNA response sequences (46,48). These previous reports indicated that some RNAs residing in animal tissues could influence functions of steroid receptors by inhibiting their interaction with DNA.…”

Section: Discussionmentioning

confidence: 99%

Noncoding RNA Gas5 Is a Growth Arrest– and Starvation-Associated Repressor of the Glucocorticoid Receptor

et al. 2010

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The availability of nutrients influences cellular growth and survival by affecting gene transcription. Glucocorticoids also influence gene transcription and have diverse activities on cell growth, energy expenditure, and survival. We found that the growth arrest-specific 5 (Gas5) noncoding RNA, which is abundant in cells whose growth has been arrested due to lack of nutrients or growth factors, sensitized cells to apoptosis by suppressing glucocorticoid-mediated induction of several responsive genes, including the one encoding cellular inhibitor of apoptosis 2. Gas5 bound to the DNA-binding domain of the glucocorticoid receptor (GR) by acting as a decoy "glucocorticoid response element (GRE)", thus, competing with DNA GREs for binding to the GR. We conclude that Gas5 is a riborepressor of the GR, influencing cell survival and metabolic activities during starvation by modulating the transcriptional activity of the GR.

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Section: Discussionmentioning

confidence: 99%

Noncoding RNA Gas5 Is a Growth Arrest– and Starvation-Associated Repressor of the Glucocorticoid Receptor

et al. 2010

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“…In spite of this, only a rather limited number of studies on the role of RNA in receptor structure have appeared in the ensuing years. However, RNA has been implicated in the structure of many steroid receptors, including those for glucocorticoids (Liao et al, 1980;Chong & Lippman, 1982;Hutchens et al, 1982;Rossini & Barbiroli, 1983;Tymoczko & Phillips, 1983;Tymoczko et al, 1984), estrogens (Liao et al, 1973(Liao et al, , 1980Liang & Liao, 1974;Chong & Lippman, 1982), androgens (Liao et al, 1973(Liao et al, , 1980Haase et al, 1983), progestins (Liao et al, 1980), and the sterol vitamin D (Franceschi & DeLuca, 1979;Franceschi et al, 1983;Franceschi, 1984). Most of these studies have involved treating crude cytosolic receptors with ribonuclease and observing a shift in receptor sedimentation rate or a change in DNA-cellulose binding activity.…”

Section: Discussionmentioning

confidence: 99%

Ribonucleic acid is a component of the oligomeric, transformed mouse AtT-20 cell glucocorticoid receptor

Kovac̆ic̆-Milivojević¹,

LaPointe²,

Reker³

et al. 1985

Biochemistry

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The glucocorticoid receptor from mouse AtT-20 pituitary tumor cells exists in three forms. The largest form is an untransformed (non-DNA-binding), oligomeric species (9.1 S, 8.3 nm, Mr 319 000). Two transformed (DNA-binding) forms can be generated. One is an oligomeric protein (5.2 S, 6-8.3 nm, Mr 132 000-182 000), while the other is the monomeric, hormone-binding subunit (3.8 S, 6 nm, Mr 96 000). The composition of the oligomeric, transformed receptor and its relationship to the monomeric protein were examined. The 3.8S monomer can be isolated from DEAE-cellulose (0.12 M step elution) in a form that continues to sediment at about 3.8 S on molybdate-containing sucrose gradients and at about 4.2 S on molybdate-free gradients. Addition of a non-hormone-binding component isolated from the same DEAE-cellulose column (0.5 M KCl step) can apparently interact with the 3.8-4.2 S monomer, increasing its sedimentation coefficient to 5.2 S (on molybdate-containing gradients) or 6.6 S (on low-salt, molybdate-free gradients). This factor is a macromolecule (nondialyzable) and is heat-stable (100 degrees C, 20 min). A dose-dependent shift to the higher sedimentation coefficient is observed when increasing quantities of the 0.5 M step material are added to the receptor monomer. This activity is abolished when the 0.5 M step material is treated with ribonuclease A. Further, when RNA is purified from the 0.5 M step by phenol/chloroform extraction, its ability to increase the S value of the monomer is retained. Ribonuclease treatment of the untransformed, 9.1S, oligomeric complex does not cause a significant decrease in sedimentation rate, while the same treatment of the 5.2S, oligomeric, transformed receptor (obtained after Sephadex G-25 transformation) causes a decrease in sedimentation rate to about 3.8 S. The addition of bovine liver mRNA and rRNA does not cause a shift in sedimentation rate of the receptor monomer to a discrete, higher sedimenting receptor form. However, the addition of total rabbit liver tRNA or three distinct tRNA species causes a shift in sedimentation to a similar, but not identical, form as that with the 0.5 M step material. We propose that the 5.2S, oligomeric transformed glucocorticoid receptor is composed of one monomeric hormone-binding, protein subunit (Mr 96 000) and a low molecular weight RNA (Mr 36 000). This interaction may be important for the role of the receptor in regulating gene expression.

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“…Numerous studies have suggested a homotetramer-homodimer-monomer model for the unactivated receptor (Raaka & Samuels, 1983;Vedeckis, 1983;Holbrook et al, 1983; 0006-2960/86/0425-5955S01.50/0 © 1986 American Chemical Society Sherman et al, 1983), while others have suggested that nonhormone binding proteins may also be components of the oligomeric forms (Grandics et al, 1984b;Gehring & Arndt, 1985;Joab et al, 1985). It has also been speculated that RNA may play a role in the structure and function of many steroid receptors including those for glucocorticoids (Liao et al, 1980; Chong & Lippman, 1982;Hutchens et al, 1982;Rossini & Barbiroli, 1983; Tymoczko & Phillips, 1983;Tymoczko et al, 1984; Economidis & Rousseau, 1985), progestins (Liao et al, 1980), androgens (Liao, 1980;Haase et al, 1983), estrogens (Liao et al, 1980; Liang & Liao, 1974;Chong & Lippman, 1982;Thomas & Kiang, 1985), and vitamin D (Franceschi & DeLuca, 1979;Franceschi et al, 1983;Franceschi, 1984).…”

mentioning

confidence: 99%

Effects of bovine pancreatic ribonuclease A, S protein, and S peptide on activation of purified rat hepatic glucocorticoid-receptor complexes

Schmidt¹,

Diehl²,

Davidson³

et al. 1986

Biochemistry

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Bovine pancreatic ribonuclease (RNase) A and S protein (enzymatically inactive proteolytic fragment of RNase A which contains RNA binding site) stimulate the activation, as evidenced by increasing DNA-cellulose binding, of highly purified rat hepatic glucocorticoid-receptor complexes. These effects are dose dependent with maximal stimulation of DNA-cellulose binding being detected at approximately 500 micrograms (50 units of RNase A/mL). RNase A and S protein do not enhance DNA-cellulose binding via their ability to interact directly with DNA or to increase nonspecific binding of receptors to cellulose. Neither S peptide (enzymatically inactive proteolytic fragment which lacks RNA binding site) nor cytochrome c, a nonspecific basic DNA binding protein, mimics these effects. RNase A and S protein do not stimulate the conformational change which is associated with activation and is reflected in a shift in the elution profile of receptor complexes from DEAE-cellulose. In contrast, these two proteins interact with previously heat-activated receptor complexes to further enhance their DNA-cellulose binding capacity and thus mimic the effects of an endogenous heat-stable cytoplasmic protein(s) which also function(s) during step 2 of in vitro activation [Schmidt, T. J., Miller-Diener, A., Webb, M. L., & Litwack, G. (1985) J. Biol. Chem. 260, 16255-16262]. Preadsorption of RNase A and S protein to an RNase affinity resin containing an inhibitory RNA analogue, or trypsin digestion of the RNA binding site within S protein, eliminates the subsequent ability of these two proteins to stimulate DNA-cellulose binding of the purified receptors.(ABSTRACT TRUNCATED AT 250 WORDS)

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Effects of RNA and ribonuclease on the binding of estrogen and glucocorticoid receptors from MCF-7 cells to DNA-cellulose.

Cited by 90 publications

References 17 publications

Noncoding RNA Gas5 Is a Growth Arrest– and Starvation-Associated Repressor of the Glucocorticoid Receptor

Noncoding RNA Gas5 Is a Growth Arrest– and Starvation-Associated Repressor of the Glucocorticoid Receptor

Ribonucleic acid is a component of the oligomeric, transformed mouse AtT-20 cell glucocorticoid receptor

Effects of bovine pancreatic ribonuclease A, S protein, and S peptide on activation of purified rat hepatic glucocorticoid-receptor complexes

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