FB2025_01 , released February 20, 2025
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Citation
Vogtli, M., Elke, C., Imhof, M.O., Lezzi, M. (1998). High level transactivation by the ecdysone receptor complex at the core recognition motif.  Nucleic Acids Res. 26(10): 2407--2414.
FlyBase ID
FBrf0102578
Publication Type
Research paper
Abstract
Ecdysteroid signaling in insects is mediated by the ecdysone receptor complex that is composed of a heterodimer of the ecdysone receptor and Ultraspiracle. The DNA binding specificity plays a critical role of defining the repertoire of target genes that respond to the hormone. We report here the determination of the preferred core recognition motif by a binding site selection procedure. The consensus sequence consists of a perfect palindrome of the heptameric half-site sequence GAGGTCA that is separated by a single A/T base pair. No binding polarity of the ecdysone receptor/Ultraspiracle heterodimer to the core recognition motif was observed. This core motif mediated the highest level of ligand-induced transactivation when compared to a series of synthetic ecdysone response elements and to the natural element of the Drosophila hsp27 gene. This is the first report of a palindromic sequence identified as the highest affinity DNA binding site for a heterodimeric nuclear hormone receptor complex. We further present evidence that the ligand of the ecdysone receptor preferentially drives Ultraspiracle from a homodimer into a heterodimer. This mechanism might contribute additionally to a tight control of target gene expression.
PubMed ID
PubMed Central ID
PMC147576 (PMC) (EuropePMC)
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Secondary IDs
    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Nucleic Acids Res.
    Title
    Nucleic Acids Research
    Publication Year
    1974-
    ISBN/ISSN
    0305-1048
    Data From Reference
    Genes (3)