Structure and Dynamic Properties of a Glucocorticoid Receptor-Induced Chromatin Transition

Fletcher, Terace M.; Ryu, Byung-Woo; Baumann, Chris; Warren, Barbour S.; Fragoso, Gilberto; John, Sam; Hager, Gordon L.

doi:10.1128/mcb.20.17.6466-6475.2000

Cited by 86 publications

(70 citation statements)

References 55 publications

(62 reference statements)

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“…Their joint action allows for the binding to DNA of a transcriptional activator (NF-1) whose binding site was previously occluded by a translationally positioned nucleosome (Archer et al, 1992), and transcription begins. An additional attractive parallel between HO and the MMTV LTR is in the transient liaison that the activator has with its target promoter: Swi5p leaves the DNA in 5 min (Cosma et al, 1999), and GR shuttles on and o DNA on a timescale of seconds (McNally et al, 2000) ± an interesting possibility with some experimental support (Fletcher et al, 2000) is that the remodeling action of SWI/SNF displaces from the DNA the very activator that targets it (Urnov and Wol e, 2001). …”

Section: Ho Endonuclease Gene Activation: Mating As Serious Businessmentioning

confidence: 99%

Chromatin remodeling and transcriptional activation: the cast (in order of appearance)

2001

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The number of chromatin modifying and remodeling complexes implicated in genome control is growing faster than our understanding of the functional roles they play. We discuss recent in vitro experiments with biochemically de®ned chromatin templates that illuminate new aspects of action by histone acetyltransferases and ATPdependent chromatin remodeling engines in facilitating transcription. We review a number of studies that present an`ordered recruitment' view of transcriptional activation, according to which various complexes enter and exit their target promoter in a set sequence, and at speci®c times, such that action by one complex sets the stage for the arrival of the next one. A consensus emerging from all these experiments is that the joint action by several types of chromatin remodeling machines can lead to a more profound alteration of the infrastructure of chromatin over a target promoter than could be obtained by these enzymes acting independently. In addition, it appears that in speci®c cases one type of chromatin structure alteration (e.g., histone hyperacetylation) is contingent upon prior alterations of a di erent sort (i.e., ATP-dependent remodeling of histone-DNA contacts). The striking di erences between the precise sequence of action by various cofactors observed in these studies may be ± at least in part ± due to di erences between the speci®c promoters studied, and distinct requirements exhibited by speci®c loci for chromatin remodeling based on their pre-existing nucleoprotein architecture. Oncogene (2001) 20, 2991 ± 3006.

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Section: Ho Endonuclease Gene Activation: Mating As Serious Businessmentioning

confidence: 99%

Chromatin remodeling and transcriptional activation: the cast (in order of appearance)

2001

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“…The GR has been shown in vitro to stimulate BRG1 chromatin remodeling using partially puri®ed complexes from either HeLa cells or from rat liver tissue (Ostlund Farrants et al, 1997). On MMTV LTR DNA reconstituted into polynucleosome arrays with Drosophila embryo extracts, puri®ed GR required ATP and HeLa nuclear extract to induce chromatin remodeling (Fletcher et al, 2000). Yeast Swi/Snf stimulated transcription via the N-terminal transactivation domain of the GR, tl, from assembled chromatin templates (Wallberg et al, 2000).…”

Section: Gr and Chromatin-remodeling Complexesmentioning

confidence: 99%

Glucocorticoid receptor-mediated chromatin remodeling in vivo

Deroo

Archer

2001

Oncogene

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The compaction of DNA into chromatin provides an additional level of gene regulation in eukaryotes that may not be available to prokaryotes. When packaged as chromatin, most promoters are transcriptionally repressed, and transcription factors have reduced access to their binding sites. The glucocorticoid receptor (GR) is a ligand-activated transcription factor that regulates the activity of genes involved in many physiological processes. To regulate eukaryotic genes, the GR binds to target sites within promoter regions of genes assembled as chromatin. This interaction alters the nucleosomal architecture to allow binding of other transcription factors, and formation of the preinitiation complex. The mouse mammary tumor virus (MMTV) promoter has been used extensively as a model to explore the processes by which the GR remodels chromatin and activates transcription. Signi®cant progress has been made in our understanding of the mechanisms used by the GR to modify chromatin structure, and the limits placed on the GR by post-translational modi®cations of histones. We will describe recent developments in the processes used by the GR to activate transcription in vivo via chromatin remodeling complexes, histone H1 phosphorylation, and recruitment of diverse coactivators. Oncogene (2001) 20, 3039 ± 3046.

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“…The latter scenario has precedent in other nuclear receptor studies. Glucocorticoid receptor-mediated remodeling of a reconstituted mouse mammary tumor virus nucleosomal array has been shown to require ATP and remodeling factors, as well as interaction with acetyltransferase coactivators, supporting the idea of distinct requirements for each of these two remodeling mechanisms (10,11). The estrogen and retinoic acid receptors also have been shown to require ATP-dependent remodeling complexes in the chromatin context (49,50).…”

Section: Discussionmentioning

confidence: 87%

“…The role of ATP-dependent mechanisms such as SWI/SNF, Mi2/NURD, and ISWI (5) in nuclear receptor-mediated regulation has also been demonstrated. Studies using the glucocorticoid receptor on the mouse mammary tumor virus promoter, which has been shown to have positioned nucleosomes (6), have demonstrated a requirement for SWI-SNF complexes and their ligand-induced targeting to the promoter to activate gene expression (7)(8)(9)(10)(11). More recently, it has been demonstrated that glucocorticoid receptor activation induces nucleosome translational positioning on the mouse mammary tumor virus promoter (12).…”

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confidence: 99%

Chromatin Remodeling by the Thyroid Hormone Receptor in Regulation of the Thyroid-stimulating Hormone α-Subunit Promoter

Collingwood¹,

Urnov²,

Chatterjee³

et al. 2001

Journal of Biological Chemistry

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The chromatin architecture of a promoter is an important determinant of its transcriptional response. For most target genes, the thyroid hormone receptor (TR) activates gene expression in response to thyroid hormone (T 3 ). In contrast, the thyroid-stimulating hormone ␣-subunit (TSH␣) gene promoter is down-regulated by TR in the presence of T 3 . Here we utilize the capacity for the Xenopus oocyte to chromatinize exogenous nuclearinjected DNA to analyze the chromatin architecture of the TSH␣ promoter and how this changes upon TR-mediated regulation. Interestingly, in the oocyte, the TSH␣ promoter was positively regulated by T 3 . In the inactive state, the promoter contained six loosely positioned nucleosomes. The addition of TR/retinoid X receptor together had no effect on the chromatin structure, but the inclusion of T 3 induced strong positioning of a dinucleosome in the TSH␣ proximal promoter that was bordered by regions that were hypersensitive to cleavage by methidiumpropyl EDTA. We identified a novel thyroid response element that coincided with the proximal hypersensitive region. Furthermore, we examined the consequences of mutations in TR that impaired coactivator recruitment. In a comparison with the Xenopus TR␤A promoter, we found that the effects of these mutations on transactivation and chromatin remodeling were significantly more severe on the TSH␣ promoter.The molecular mechanism of nuclear hormone receptor-mediated gene regulation and the importance of chromatin structure to this process have been intensively investigated over the past decade. Although the packaging of DNA into dense chromatin is a barrier to transcription factor access, multiple mechanisms exist to overcome this obstacle and thereby facilitate regulation of gene expression (1-3). Regulation of the acetylation state of core nucleosomal histone proteins influences their interaction with DNA and, subsequently, the nucleosomal packing density and transcription factor accessibility to chromatin. Transcriptional repression by DNA-bound thyroid hormone receptor (TR) 1 in the absence of hormone (T 3 ) involves the recruitment of histone deacetylase-containing complexes that facilitate the formation of repressive chromatin structure. The addition of T 3 causes the release of the deacetylase complexes and stimulates transcriptional activation by the recruitment of coactivators that include acetyltransferase components (1-3). The acetyltransferases and deacetylases are numerous, but occur in discrete subcomplexes that may exhibit cell type and promoter context dependence (4). The role of ATP-dependent mechanisms such as SWI/SNF, Mi2/NURD, and ISWI (5) in nuclear receptor-mediated regulation has also been demonstrated. Studies using the glucocorticoid receptor on the mouse mammary tumor virus promoter, which has been shown to have positioned nucleosomes (6), have demonstrated a requirement for SWI-SNF complexes and their ligand-induced targeting to the promoter to activate gene expression (7-11). More recently, it has been demonstrated tha...

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Structure and Dynamic Properties of a Glucocorticoid Receptor-Induced Chromatin Transition

Cited by 86 publications

References 55 publications

Chromatin remodeling and transcriptional activation: the cast (in order of appearance)

Chromatin remodeling and transcriptional activation: the cast (in order of appearance)

Glucocorticoid receptor-mediated chromatin remodeling in vivo

Chromatin Remodeling by the Thyroid Hormone Receptor in Regulation of the Thyroid-stimulating Hormone α-Subunit Promoter

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