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Mutational analysis of the interaction between ecdysteroid receptor and its response element.

作者信息

Oźyhar A, Pongs O

机构信息

Technical University of Wroclaw, Institute of Organic and Physical Chemistry, Poland.

出版信息

J Steroid Biochem Mol Biol. 1993 Aug;46(2):135-45. doi: 10.1016/0960-0760(93)90288-8.

DOI:10.1016/0960-0760(93)90288-8
PMID:8664161
Abstract

The interaction between the partially purified ecdysteroid receptor (EcR) and the mutated ecdysteroid-response element (EcRE) from the hsp27 gene promoter was studied using the gel retardation competition assay. The results suggest that the EcR-hsp27 EcRE contact sites are made predominantly by base pairs which are at positions -7, -6, -5, -2, -1 and +2, +5, +6 of the hsp27 EcRE palindrome. An increase or decrease in the spacing between the half-palindromes reduces the affinity of the hsp27 EcRE to the receptor, while a mutation of the central A/T base pair to C/G has practically no effect on EcR binding. Unlike the glucocorticoid-response element and the estrogen-response element, the base pairs placed at positions -3, -4 and +1, +3, +4 of the hsp27 EcRE palindrome can be mutated without effect on the EcR binding.

摘要

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