Evaluation of simultaneous binding of Chromomycin A3 to the multiple sites of DNA by the new restriction enzyme assay

Hirotaka Murase, Tomoharu Noguchi, Shigeki Sasaki

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


Chromomycin A3 (CMA3) is an aureolic acid-type antitumor antibiotic. CMA3 forms dimeric complexes with divalent cations, such as Mg2+, which strongly binds to the GC rich sequence of DNA to inhibit DNA replication and transcription. In this study, the binding property of CMA3 to the DNA sequence containing multiple GC-rich binding sites was investigated by measuring the protection from hydrolysis by the restriction enzymes, AccII and Fnu4HI, for the center of the CGCG site and the 5′-GC↓GGC site, respectively. In contrast to the standard DNase I footprinting method, the DNA substrates are fully hydrolyzed by the restriction enzymes, therefore, the full protection of DNA at all the cleavable sites indicates that CMA3 simultaneously binds to all the binding sites. The restriction enzyme assay has suggested that CMA3 has a high tendency to bind the successive CGCG sites and the CGG repeat.

Original languageEnglish
Pages (from-to)1832-1835
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Issue number10
Publication statusPublished - 2018 Jun 1


  • AccII
  • CGG repeat
  • Chromomycin A3
  • Fnu4HI
  • Multiple CGCG sites

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry


Dive into the research topics of 'Evaluation of simultaneous binding of Chromomycin A<sub>3</sub> to the multiple sites of DNA by the new restriction enzyme assay'. Together they form a unique fingerprint.

Cite this