Specific binding of progesterone receptor to progesterone-responsive elements does not require prior dimerization.
Eur J Biochem
; 214(1): 189-95, 1993 May 15.
Article
em En
| MEDLINE
| ID: mdl-7685278
ABSTRACT
Steroid-hormone receptors undergo, prior to binding to DNA, a hormone-dependent dimerization. It is generally accepted that this dimerization is indispensable for the high-affinity binding of hormone receptor to hormone-responsive elements. Using a progesterone-receptor mutant with the complete steroid-binding domain deleted (positions 663-930), with or without the epitope required for binding the monoclonal antibody Let 126, we have shown that this receptor species was unable to undergo dimerization in solution. However, this mutant retained a high affinity (60-70% of the affinity of the wild-type receptor) for the progesterone-responsive elements of the mouse-mammary-tumor-virus long-terminal-repeat promoter and for a consensus palindromic progesterone-responsive element, as measured by both DNase-I protection experiments and gel-shift experiments. This mutant also increased gene transcription. Thus, at least in the case of the progesterone receptor, prior dimerization is dispensable for receptor binding to regulatory DNA elements and for subsequent transcription activation.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
DNA Viral
/
Receptores de Progesterona
/
Sequências Reguladoras de Ácido Nucleico
/
Vírus do Tumor Mamário do Camundongo
Limite:
Animals
Idioma:
En
Revista:
Eur J Biochem
Ano de publicação:
1993
Tipo de documento:
Article