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J. Biol. Chem., Vol. 276, Issue 36, 34227-34234, September 7, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/36/34227    most recent M105172200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Collingwood, T. N. Articles by Wolffe, A. P. Search for Related Content PubMed PubMed Citation Articles by Collingwood, T. N. Articles by Wolffe, A. P. Social Bookmarking                      What's this?

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

Trevor N. Collingwood^§, Fyodor D. Urnov^¶, V. Krishna K. Chatterjee, and Alan P. Wolffe^¶

From the  Laboratory of Molecular Embryology, National Institutes of Health, Bethesda, Maryland 20892 and the  Department of Medicine, Addenbrookes Hospital, University of Cambridge, Cambridge CB2 2QQ, United Kingdom

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 (T₃). In contrast, the thyroid-stimulating hormone -subunit (TSH) gene promoter is down-regulated by TR in the presence of T₃. Here we utilize the capacity for the Xenopus oocyte to chromatinize exogenous nuclear- injected 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 T₃. 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 T₃ 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 TRA promoter, we found that the effects of these mutations on transactivation and chromatin remodeling were significantly more severe on the TSH promoter.

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