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参与配体激活DNA识别的芳烃受体结构域的体外分析。

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

作者信息

Dolwick K M, Swanson H I, Bradfield C A

机构信息

Department of Pharmacology, Northwestern University Medical School, Chicago, IL 60611.

出版信息

Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8566-70. doi: 10.1073/pnas.90.18.8566.

DOI:10.1073/pnas.90.18.8566
PMID:8397410
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC47398/
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.

摘要

芳烃受体(AHR)是一种碱性螺旋-环-螺旋蛋白,介导2,3,7,8-四氯二苯并对二恶英的效应。在本报告中,我们描述了一种兔网织红细胞系统,该系统能够使AHR及其二聚体伴侣——芳烃受体核转运蛋白(ARNT)进行功能性表达。通过使用这个体外系统,我们能够重建激动剂与AHR的结合以及激动剂诱导的AHR-ARNT对同源DNA增强子序列的识别。AHR缺失突变体的表达揭示了负责配体和DNA识别的N端结构域以及在激动剂诱导的DNA识别中起作用的C端结构域的位置。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e3b9/47398/0f7c654fe244/pnas01475-0273-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e3b9/47398/af21329a7d11/pnas01475-0271-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e3b9/47398/bac79b96a3df/pnas01475-0272-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e3b9/47398/0f7c654fe244/pnas01475-0273-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e3b9/47398/af21329a7d11/pnas01475-0271-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e3b9/47398/bac79b96a3df/pnas01475-0272-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e3b9/47398/0f7c654fe244/pnas01475-0273-a.jpg

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