Possible function of Ah receptor nuclear translocator (Arnt) homodimer in transcriptional regulation

Kazuhiro Sogawa, Ryosuke Nakano, Akira Kobayashi, Yasuo Kikuchi, Norihisa Ohe, Natsuki Matsushita, Yoshiaki Fujii-Kuriyama

Research output: Contribution to journalArticlepeer-review

168 Citations (Scopus)

Abstract

Arnt (Ah receptor nuclear translocator) is a member of a transcription factor family having characteristic motifs designated bHLH (basic helix- loop-helix) and PAS and was originally found as a factor forming a complex with Ah receptor (AhR) to bind the specific xenobiotic responsive element (XRE) sequence for induction of drug-metabolizing P4501A1. We have examined interaction of Arnt with other PAS proteins Drosophila Per, Sim, and AhR by the coimmunoprecipitation method. Arnt formed a homodimer with itself as well as heterodimers with the others by means of the PAS and HLH domains in a cooperative way. The Arnt homodimer binds the sequence of adenovirus major late promoter (MLP) with the E box core sequence CACGTG, suggesting that the CAC half of the XRE, CACGCN(A/T), recognized by the AhR-Arnt heterodimer is a target for Arnt. Cotransfection experiments using CV-1 cells with an Arnt expression plasmid and a MLP chloramphenicol acetyltransferase (CAT) reporter plasmid revealed that Arnt markedly activated CAT expression, indicative of a newly discovered regulatory role of Arnt.

Original languageEnglish
Pages (from-to)1936-1940
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume92
Issue number6
DOIs
Publication statusPublished - 1995 Mar 14
Externally publishedYes

Keywords

  • P4501A1
  • PAS domain
  • basic helix-loop-helix domain

ASJC Scopus subject areas

  • General

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