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In vitro analysis of Ah receptor domains involved in ligand-activated DNA recognition.


ABSTRACT: 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.

SUBMITTER: Dolwick KM 

PROVIDER: S-EPMC47398 | biostudies-other | 1993 Sep

REPOSITORIES: biostudies-other

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In vitro analysis of Ah receptor domains involved in ligand-activated DNA recognition.

Dolwick K M KM   Swanson H I HI   Bradfield C A CA  

Proceedings of the National Academy of Sciences of the United States of America 19930901 18


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  ...[more]

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