In vitro analysis of Ah receptor domains involved in ligand-activated DNA recognition.
AUTOR(ES)
Dolwick, K M
RESUMO
The Ah receptor (AHR) is a basic helix-loop-helix protein that mediates the effects of 2,3,7,8-tetrachloro-dibenzo-p-dioxin. In this report, we describe a rabbit reticulocyte system that allows functional expression of both the AHR and its dimeric partner, the AHR nuclear translocator protein (ARNT). By using this in vitro system, we were able to reconstitute agonist binding to the AHR and agonist-induced AHR-ARNT recognition of a cognate DNA enhancer sequence. Expression of AHR deletion mutants revealed the location of N-terminal domains responsible for ligand and DNA recognition and C-terminal domains that play roles in agonist-induced DNA recognition.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=47398Documentos Relacionados
- Cloning of the Ah-receptor cDNA reveals a distinctive ligand-activated transcription factor.
- Ligand-activated site-specific recombination in mice.
- The Orphan Nuclear Receptor SHP Utilizes Conserved LXXLL-Related Motifs for Interactions with Ligand-Activated Estrogen Receptors
- The Major Human Pregnane X Receptor (PXR) Splice Variant, PXR.2, Exhibits Significantly Diminished Ligand-Activated Transcriptional RegulationS⃞
- Natural killer-like nonspecific tumor cell lysis mediated by specific ligand-activated Vα14 NKT cells