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Structural and functional features of a specific nucleosome containing a recognition element for the thyroid hormone receptor
Author(s) -
Wong Jiemin,
Li Qiao,
Levi BenZion,
Shi YunBo,
Wolffe Alan P.
Publication year - 1997
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/16.23.7130
Subject(s) - biology , nucleosome , thyroid hormone receptor , thyroid , receptor , hormone , hormone response element , hormone receptor , computational biology , endocrinology , genetics , dna , histone , estrogen receptor , cancer , breast cancer
The Xenopus thyroid hormone receptor βA (TRβA) gene contains an important thyroid hormone response element (TRE) that is assembled into a positioned nucleosome. We determine the translational position of the nucleosome containing the TRE and the rotational positioning of the double helix with respect to the histone surface. Histone H1 is incorporated into the nucleosome leading to an asymmetric protection to micrococcal nuclease cleavage of linker DNA relative to the nucleosome core. Histone H1 association is without significant consequence for the binding of the heterodimer of thyroid hormone receptor and 9‐ cis retinoic acid receptor (TR/RXR) to nucleosomal DNA in vitro , or for the regulation of TRβA gene transcription following microinjection into the oocyte nucleus. Small alterations of 3 and 6 bp in the translational positioning of the TRE in chromatin are also without effect on the transcriptional activity of the TRβA gene, whereas a small change in the rotational position of the TRE (3 bp) relative to the histone surface significantly reduces the binding of TR/RXR to the nucleosome and decreases transcriptional activation directed by TR/RXR. Our results indicate that the specific architecture of the nucleosome containing the TRE may have regulatory significance for expression of the TRβA gene.