The Affinity of Nuclear Factor 1 for Its DNA Site Is Drastically Reduced by Nucleosome Organization Irrespective of Its Rotational or Translational Position

Blomquist, Patrik; Li, Qiao; Wränge, Örjan

doi:10.1074/jbc.271.1.153

Cited by 86 publications

(74 citation statements)

References 52 publications

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“…Previous work suggested that the nucleosome positioning is important for restricting the access of NF1, Oct1, and other basal factors to their cognate binding sites, as shown in vitro for NF1 (17,57,58). During hormone induction, it was assumed that the hormone-activated GR binds and mediates a chromatin-remodeling event that will then allow binding of NF1, Oct1, and other basal factors to the MMTV promoter.…”

Section: The Mechanism Of Nucleosome Positioning Of the Mmtv Ltr: Intmentioning

confidence: 99%

Nuclear Factor 1 and Octamer Transcription Factor 1 Binding Preset the Chromatin Structure of the Mouse Mammary Tumor Virus Promoter for Hormone Induction

Беликов

Holmqvist

Åstrand

et al. 2004

Journal of Biological Chemistry

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When the mouse mammary tumor virus (MMTV) is integrated into the genome of a mammalian cell, its long terminal repeat (LTR) harbors six specifically positioned nucleosomes. Transcription from the MMTV promoter is regulated by the glucocorticoid hormone via the glucocorticoid receptor (GR). The mechanism of the apparently constitutive nucleosome arrangement has remained unclear. Previous in vitro reconstitution of nucleosome(s) on small segments of the MMTV LTR suggested that the DNA sequence was decisive for the nucleosome arrangement. However, microinjection of MMTV LTR DNA in Xenopus oocytes rendered randomly distributed nucleosomes. This indicated that oocytes lack factor(s) that induces nucleosome positioning at the MMTV LTR in other cells. Here we demonstrate that specific and concomitant binding of nuclear factor 1 (NF1) and octamer factor 1 (Oct1) to their cognate sites within the MMTV promoter induce a partial nucleosome positioning that is an intermediary state between the randomly organized inactive promoter and the hormone and GR-activated promoter containing distinctly positioned nucleosomes. Oct1 and NF1 reciprocally facilitate each other's binding to the MMTV LTR in vivo. The NF1 and Oct1 binding also facilitate hormone-dependent GR-DNA interaction and result in a faster and stronger hormone response. Since NF1 and Oct1 generate an intermediary state of nucleosome positioning and enhance the hormone-induced response, we refer to this as a preset chromatin structure. We propose that this state of NF1 and Oct1-induced chromatin presetting mimics the early step(s) of chromatin remodeling involved in tissue-specific gene expression.

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Section: The Mechanism Of Nucleosome Positioning Of the Mmtv Ltr: Intmentioning

confidence: 99%

Nuclear Factor 1 and Octamer Transcription Factor 1 Binding Preset the Chromatin Structure of the Mouse Mammary Tumor Virus Promoter for Hormone Induction

Беликов

Holmqvist

Åstrand

et al. 2004

Journal of Biological Chemistry

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“…This results in a tighter chromatin structure which confers a more stringent repression of transcription than chromatin formed on DNA injected in the double-stranded form (2). Several studies suggest that chromatin acts both by excluding certain upstreamgene-specific transcription factors from their recognition sites (1,4) and by inhibiting access of the basic transcription machinery to the transcriptional initiation site (17,30,33,64).…”

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confidence: 99%

Glucocorticoid Receptor-Glucocorticoid Response Element Binding Stimulates Nucleosome Disruption by the SWI/SNF Complex

Farrants

Blomquist

Kwon

et al. 1997

Molecular and Cellular Biology

139

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The organization of DNA in chromatin is involved in repressing basal transcription of a number of inducible genes. Biochemically defined multiprotein complexes such as SWI/SNF (J. Côté, J. Quinn, J. L. Workman, and C. L. Peterson, Science 265:53-60, 1994) and nucleosome remodeling factor (T. Tsukiyama and C. Wu, Cell 83:1011-1020, 1995) disrupt nucleosomes in vitro and are thus candidates for complexes which cause chromatin decondensation during gene induction. In this study we show that the glucocorticoid receptor (GR), a hormone-inducible transcription factor, stimulates the nucleosome-disrupting activity of the SWI/SNF complex partially purified either from HeLa cells or from rat liver tissue. This GR-mediated stimulation of SWI/SNF nucleosome disruption depended on the presence of a glucocorticoid response element. The in vitro-reconstituted nucleosome probes used in these experiments harbored 95 bp of synthetic DNA-bending sequence in order to rotationally position the DNA. The GR-dependent stimulation of SWI/SNF-mediated nucleosome disruption, as evaluated by DNase I footprinting, was 2.7-to 3.8-fold for the human SWI/SNF complex and 2.5-to 3.2-fold for the rat SWI/SNF complex. When nuclear factor 1 (NF1) was used instead of GR, there was no stimulation of SWI/SNF activity in the presence of a mononucleosome containing an NF1 binding site. On the other hand, the SWI/SNF nucleosome disruption activity increased the access of NF1 for its nucleosomal binding site. No such effect was seen on binding of GR to its response element. Our results suggest that GR, but not NF1, is able to target the nucleosome-disrupting activity of the SWI/SNF complex.DNA in eukaryotic cells associates with proteins called histones to form nucleosomes, which together with nonhistone proteins form a higher-order structure, chromatin (22). It is now well established that chromatin not only provides a DNA storage function but is also involved in gene regulation (41,63). When the synthesis of histone H4 is inhibited in yeast cells, several genes which are tightly regulated are expressed in a constitutive manner (14). The mouse mammary tumor virus (MMTV) promoter, which is repressed in the absence of glucocorticoid hormone, becomes constitutively expressed when the nucleosome density is decreased by coinjection of competitor DNA, as shown in Xenopus oocytes (43). Injection of single-stranded DNA into Xenopus oocytes leads to nucleosome assembly coupled to DNA synthesis. This results in a tighter chromatin structure which confers a more stringent repression of transcription than chromatin formed on DNA injected in the double-stranded form (2). Several studies suggest that chromatin acts both by excluding certain upstreamgene-specific transcription factors from their recognition sites (1, 4) and by inhibiting access of the basic transcription machinery to the transcriptional initiation site (17,30,33,64).Regulatory regions of many inducible genes in mammals and yeast have positioned nucleosomes. Examples include the MMTV promoter (53), the...

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“…Activation of the MMTV promoter by steroid hormones is associated with a region-specific chromatin structural transition detected as an increase in sensitivity to nucleases (38,39), chemical probes (38), or restriction enzymes (1). This nucleoprotein remodeling event is implicated, in turn, in the secondary binding of transcription factors that are excluded by nonremodeled chromatin (2,4,8,22,37,(45)(46)(47).…”

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confidence: 99%

“…Glucocorticoid receptor (GR)-induced remodeling was originally associated with one nucleosome family (Nuc-B) in the LTR-phased array (1,4,22,37,38,46,47); four receptor binding sites are associated with this nucleosome family (Ϫ70 to Ϫ190). Recently, however, the region of GR-induced hypersensitivity has been found to extend upstream of the Nuc-B region to Ϫ295 (15).…”

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confidence: 99%

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

Fletcher

Ryu²,

Baumann

et al. 2000

Molecular and Cellular Biology

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Activation of the mouse mammary tumor virus (MMTV) promoter by the glucocorticoid receptor (GR) is18:3633-3644). We have reconstituted MMTV LTR DNA into a polynucleosome array using Drosophila embryo extracts. We show binding of purified GR to specific GR elements within a large, multinucleosome array and describe a GR-induced nucleoprotein transition that is dependent on ATP and a HeLa nuclear extract. Previously uncharacterized GR binding sites in the upstream C nucleosome region are involved in the extended region of chromatin remodeling. We also show that GR-dependent chromatin remodeling is a multistep process; in the absence of ATP, GR binds to multiple sites on the chromatin array and prevents restriction enzyme access to recognition sites. Upon addition of ATP, GR induces remodeling and a large increase in access to enzymes sites within the transition region. These findings suggest a dynamic model in which GR first binds to chromatin after ligand activation, recruits a remodeling activity, and is then lost from the template. This model is consistent with the recent description of a "hit-and-run" mechanism for GR action in living cells

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The Affinity of Nuclear Factor 1 for Its DNA Site Is Drastically Reduced by Nucleosome Organization Irrespective of Its Rotational or Translational Position

Cited by 86 publications

References 52 publications

Nuclear Factor 1 and Octamer Transcription Factor 1 Binding Preset the Chromatin Structure of the Mouse Mammary Tumor Virus Promoter for Hormone Induction

Nuclear Factor 1 and Octamer Transcription Factor 1 Binding Preset the Chromatin Structure of the Mouse Mammary Tumor Virus Promoter for Hormone Induction

Glucocorticoid Receptor-Glucocorticoid Response Element Binding Stimulates Nucleosome Disruption by the SWI/SNF Complex

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

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