Specific binding of chartreusin, an antitumor antibiotic, to DNA

Masakazu Uramoto, Tomonobu Kusano, Tomoko Nishio, Kiyoshi Isono, Kazuo Shishido, Tadahiko Ando

    Research output: Contribution to journalArticlepeer-review

    18 Citations (Scopus)


    Chartreusin, an antitumor and antibacterial antibiotic, was found to inhibit negatively superhelical DNA-relaxation catalyzed by prokaryotic topoisomerase I and conversion of the superhelical DNA into unit length linear form catalyzed by single-strand-specific S1 nuclease. The inhibitory effect of the agent was due to the binding to DNA causing the alteration of tertiary structure. To characterize the binding specificity, we investigated the protection of DNA against cleavages by various restriction endonucleases. It was evidenced that the binding of the agent is not at random and correlates to the sequence {A figure is presented} on DNA stretch.

    Original languageEnglish
    Pages (from-to)325-328
    Number of pages4
    JournalFEBS Letters
    Issue number2
    Publication statusPublished - 1983 Mar 21


    • Antitumor antibiotic
    • Chartreusin
    • Restriction endonuclease
    • S1 nuclease
    • Specific binding to DNA
    • Topoisomerase I

    ASJC Scopus subject areas

    • Biophysics
    • Structural Biology
    • Biochemistry
    • Molecular Biology
    • Genetics
    • Cell Biology


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