Steroid Receptors: Elements for Modulation of Eukaryotic Transcription

Yamamoto, Keith R.; Alberts, Bruce

doi:10.1146/annurev.bi.45.070176.003445

Cited by 681 publications

(204 citation statements)

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“…Real-time, single cell imaging analysis of NRs showed that the NRs are highly mobile in the nucleus (Hager et al, 2004). This is consistent with prior ideas where receptors would be thought to transiently associate with high affinity binding sites as a prelude to a successful ignition of the transcriptional response (Archer et al, 1991;Rigaud et al, 1991;Yamamoto and Alberts, 1976). By the use of tandem arrays of hormone responsive promoters, NRs such as GR and interacting coactivators have been found to rapidly exchange, in the order of seconds on the target promoter, suggesting that these factors are continuously scanning the promoter in a stochastic fashion termed 'hit-and-run' (McNally et al, 2000).…”

Section: A Newtonian Ordered and Dynamic Recruitment Of Cofactorssupporting

confidence: 85%

Dynamics of coactivator recruitment and chromatin modifications during nuclear receptor mediated transcription

Archer

2008

Molecular and Cellular Endocrinology

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The mechanisms and interplay of coactivators that underlie transcription activation is a critical avenue of investigation in biology today. Using nuclear receptor mediated transcription activation as a model, the nature of coactivator recruitment and chromatin modifications have been found to be highly dynamic. Progress in understanding the kinetics and regulation of coactivator recruitment, and subsequent effects on transcriptional readout, has greatly improved our understanding of nuclear receptor mediated transcription, the subject of discussion in this 'At the Cutting Edge' review.

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Section: A Newtonian Ordered and Dynamic Recruitment Of Cofactorssupporting

confidence: 85%

Dynamics of coactivator recruitment and chromatin modifications during nuclear receptor mediated transcription

Archer

2008

Molecular and Cellular Endocrinology

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“…This suggested that lowaffinity non-specific DNA binding could preclude detection of a small number of physiologically relevant DNA binding sites, as is the case for prokaryotic transcriptional regulatory proteins (Yamamoto & Alberts, 1976). The availability of purified receptor, together with the discovery in MTV of defined DNA sequences involved in the glucocorticoid control of gene expression, made it pbssible to re-assess the issue.…”

Section: Glucocorticoids Modulate Mrna Concentrationmentioning

confidence: 99%

Control of gene expression by glucocorticoid hormones

Rousseau¹

1984

Biochemical Journal

142

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Glucocorticoids control the expression of a small number of transcriptionally active genes by increasing or decreasing mRNA concentration. Either effect can result from a transcriptional or a post-transcriptional mechanism. Induction of mouse mammary tumour virus RNA results from a stimulation of transcription initiation and depends on the presence of defined regions in proviral DNA. These regions bind the glucocorticoid receptor and behave functionally as proto-enhancers. Glucocorticoid-inducible genes can retain their sensitivity to the hormone after transfer to a heterologous cell by transfection techniques. Non-inducible genes can become inducible when linked to the promoter region of an inducible gene. The mechanisms by which the receptor-steroid complex stimulates or inhibits transcription or influences mRNA stability are unknown. Receptor binding to nucleic acids appears to be a necessary but not sufficient condition. It is likely that the receptor also interacts with chromatin proteins. This might lead to a catalytic modification of these proteins, resulting in a modulation of gene expression. Development of glucocorticoid-sensitive, biochemically defined, cell-free transcription systems should provide a tool to delineate the molecular determinants of this essential regulatory mechanism.

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“…Moreover, changes in the behavior of IgG fraction on Sephadex chromatography were observed after binding to and extracting from nuclei, but the details of the mechanism of these changes were not clear at all at the present moment. It was also reported that receptor protein showed DNA-induced receptor aggregation (Yamamoto and Alberts, 1976).…”

Section: Discussionmentioning

confidence: 96%

“…The acceptor site for the complex in nuclei was postulated as DNAassociated nonhistone protein (Wang1.978; Klyzsejko-Stefanowicz et al,, 1976). The mode of nuclear binding of hormone-receptor complex so far reported seems to be disputable (reviewed by Gorski and Gannon, 1976;Yamamoto and Alberts, 1976); the restricted and organ-specific binding was reported by Liao et al(1975), and nonspecific and unsaturable binding was described by Chamness et al(1974). Lack of tissue-specificity of the prostatic dihydrotestosterone-receptor complex binding to nuclei was also reported (Ichii, 1975;Ichii et al, 1977).…”

Section: Discussionmentioning

confidence: 99%