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

    164 Citations (Scopus)


    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
    Issue number6
    Publication statusPublished - 1995 Mar 14


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

    ASJC Scopus subject areas

    • General


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