Role of Specific Chromosomal Proteins and DNA Sequences in the Nuclear Binding Sites for Steroid Receptors

Spelsberg, TC; Ba, Littlefield; Seelke, Ralph; Gm, Dani; Toyoda, Hiroo; Boyd-Leinen, P. A.; Thrall, C. L.; Ol, Kon

doi:10.1016/b978-0-12-571139-5.50016-1

Cited by 40 publications

(68 citation statements)

References 150 publications

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“…The rapid sex steroid action on steady-state levels of the c-jun protooncogene mRNA described in this report supports the cascade model of hormone action discussed in detail above and elsewhere (5,6). The model describes a role for rapid steroid regulation of "regulatory" genes, which in this 200 240 case would be the c-jun protooncogene.…”

Section: Resultssupporting

confidence: 82%

“…In some systems, a requirement for protein synthesis during this lag period is required for the subsequent induction of the mRNA levels (3,4). A cascade model for steroid hormone action has been proposed whereby steroids rapidly regulate the expression of "early" (regulatory) genes during the lag phase (5)(6)(7)(8)(9). The products of these regulatory genes in turn regulate the expression of individual or whole groups of "late" structural genes.…”

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confidence: 99%

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Rapid induction of the c-jun protooncogene in the avian oviduct by the antiestrogen tamoxifen.

Lau

Subramaniam

Rasmussen

et al. 1991

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

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This report describes a rapid regulation of the expression of the c-jun protooncogene by the antiestrogen tamoxifen (Tam). The c-jun protooncogene codes for an important component of the AP-1 transcription factor complex, which regulates the expression of many unlinked genes. Repeated experiments have shown that Tam rapidly increases the steady-state c-jun mRNA levels in the avian oviduct but decreases the levels in the liver. The Tam effects are time- and dose-dependent. These results are supported by other studies that have demonstrated that 17 beta-estradiol decreases steady-state levels of c-jun protooncogene mRNA in oviducts of animals fully withdrawn from estradiol. The effect of Tam in the avian oviduct is in contrast to the reported effects of Tam on the expression of practically all other genes in the avian oviduct and other animal tissues. Transcription analyses using nuclear runoff experiments with oviduct nuclei demonstrate a decrease in the c-jun gene transcription within minutes after Tam treatment with a return to 75% of control values by 4 hr. The fact that Tam transiently decreases the transcription of the c-jun gene but increases the steady-state c-jun mRNA levels suggests that Tam must alter both transcriptional and post-transcriptional events. The results support a role of the c-jun protooncogene as a regulatory gene in the cascade model for steroid action whereby steroids rapidly regulate the regulatory genes, which in turn regulate many other structural genes.

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Section: Resultssupporting

confidence: 82%

mentioning

confidence: 99%

Rapid induction of the c-jun protooncogene in the avian oviduct by the antiestrogen tamoxifen.

Lau

Subramaniam

Rasmussen

et al. 1991

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

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“…Further, the capacity of the PR to bind to nuclear acceptor sites reflects the ability of progesterone to alter RNA polymerase activity in nuclear run-off experiments (17, t) and to specifically induce the avidin gene (18). A specific subset of nonhistone proteins (acceptor proteins) has been shown to be necessary for the generation of specific nucleoprotein acceptor sites (10,11,(19)(20)(21).In other organisms, similar nuclear acceptor sites composed of tightly bound (to DNA) nonhistone proteins have been reported for the estrogen receptor/chicken oviduct system (17), for systems involving the estrogen and progesterone receptors in sheep brain (22), in hamster uteri (t), in cow, rabbit, and human uteri (21, 23, 24), for systems involving the glucocorticoid receptor in both rat liver (25) and human leukemic cell line system (26), and finally for the androgen receptor rat prostate system (27). Thus, the acceptor protein-DNA complex as a potential nuclear acceptor site model for steroid receptors seems to be universal.…”

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confidence: 99%

Nuclease resistance and the enrichment of native nuclear acceptor sites for the avian oviduct progesterone receptor.

Hora¹,

Horton²,

Toft³

et al. 1986

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

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High-affinity nucleoprotein acceptor sites for the avian oviduct progesterone receptor (PR) have been enriched by a combination of nuclease digestion and centrifugation. These enriched binding elements exhibited markedly enhanced PR binding on a per mass DNA basis compared to chromatin (20-to 25-fold) or dehistonized chromatin (4-to 5-fold). Electrophoretic analysis of the nuclease-resistant DNA showed that there is a set of DNA fragments of 100-150 base pairs that are protected from digestion. Excessive digestion resulted in smaller DNA fragments and a loss of PR binding activity. The PR binding was saturable using a crude receptor preparation and displayed a competition with the same receptor preparation that was labeled with nonradioactive progesterone. The enhanced binding was also demonstrable using highly purified receptor preparations that exhibit two classes of binding sites both of which are of high affinity and saturable as assessed by Scatchard analyses. These two high-affinity classes of binding sites are shown to be competed by unlabeled purified PR. The nuclease resistance of these nucleoprotein acceptor sites from chromatin is a property similar to the nuclear matrix binding sites suggesting a relationship between these two classes of nuclear acceptor sites.Based on the presently accepted mechanism of steroid hormone action, the interaction of a steroid receptor-hormone complex with the nucleus is an important step in the induction of specific gene products. A great deal of effort has been invested by a number of laboratories in trying to determine the relevant receptor-nuclear interactions. Despite these efforts, the exact nature of the nuclear binding sites (acceptor sites) is not completely understood. Steroid receptors have been shown to bind to DNA (1), RNA (2), chromatin (3), and ribonucleoprotein particles (4).This laboratory has been concentrating on the specific interaction ofthe chicken oviduct progesterone receptor (PR) with nuclear acceptor sites in oviduct chromatin. In contrast to the receptor binding to pure DNA sequences alone (5, 6), the binding of the oviduct PR to subfractions of chromatin containing nonhistone protein-DNA complexes, termed nucleoacidic protein or NAP, has been shown to be receptor dependent and saturable, of high affinity (7)(8)(9)(10)(11), to be receptor specific (12), and to generate patterns of bindings similar to that measured in vivo (13)(14)(15)(16). Further, the capacity of the PR to bind to nuclear acceptor sites reflects the ability of progesterone to alter RNA polymerase activity in nuclear run-off experiments (17, t) and to specifically induce the avidin gene (18). A specific subset of nonhistone proteins (acceptor proteins) has been shown to be necessary for the generation of specific nucleoprotein acceptor sites (10,11,(19)(20)(21).In other organisms, similar nuclear acceptor sites composed of tightly bound (to DNA) nonhistone proteins have been reported for the estrogen receptor/chicken oviduct system (17), for systems involving the estrog...

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“…). The exact nature of the nuclear acceptor sites for Prog-receptor B is still an area of extensive investigation (Spelsberg et al, 1983). However, it would appear that progesterone-specific gene activity in chick oviduct is more closely correlated to the presence in nuclei of functional receptors B than to the existence of nuclear receptors A (Boyd-Leinen et al, 1984).…”

Section: Introductionmentioning

confidence: 99%

“…The exact nature of the « acceptor proteins », together with the mechanism by which they regulate expression of specific genes is still under extensive investigation (see Spelsberg et al, 1983).…”

Section: Introductionmentioning

confidence: 99%

Control of gene expression by steroid hormones

Béchet¹

1986

Reprod. Nutr. Dévelop.

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Role of Specific Chromosomal Proteins and DNA Sequences in the Nuclear Binding Sites for Steroid Receptors

Cited by 40 publications

References 150 publications

Rapid induction of the c-jun protooncogene in the avian oviduct by the antiestrogen tamoxifen.

Rapid induction of the c-jun protooncogene in the avian oviduct by the antiestrogen tamoxifen.

Nuclease resistance and the enrichment of native nuclear acceptor sites for the avian oviduct progesterone receptor.

Control of gene expression by steroid hormones

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