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Nucleic Acids Research, 1988, Vol. 16, No. 6 2489-2507
© 1988

Articles

Sequence-specific binding of luzopeptin to DNA

Keith R. Fox, Heather Davies, Gill R. Adams, Jose Portugal and Michael J. Waring

Department of Pharmacology, University of Cambridge Hills Road, Cambridge CB2 2QD, UK 1Department of Physiology and Pharmacology, University of Southampton Bassett Crescent East, Southampton SO9 3TU, UK

Received December 23, 1987. Revised February 19, 1988. Accepted February 19, 1988.

We have examined the binding of luzopeptin, an antitumour antibiotic, to five DNA fragments of varying base composition. The drug forms a tight, possibly covalent, complex with the DNA causing a reduction in mobility on nondenaturing polyacrylamide gels and some smearing of the bands consistent with intramolecular cross-linking of DNA duplexes. DNAaseI and micrococcal nuclease footprinting experiments suggest that the drug binds best to regions containing alternating A and T residues, although no consensus di- or trinucleotide sequence emerges. Binding to other sites is not excluded and at moderate ligand concentrations the DNA is almost totally protected from enzyme attack. Ligand-induced enhancement of DNAaseI cleavage is observed at both AT and GC-rich regions. The sequence selectivity and characteristics of luzopeptin binding are quite different from those of echinomycin, a bifunctional intercalator of related structure.


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