Sequence-specific binding of luzopeptin to DNA
Sequence-specific binding of luzopeptin to DNA
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.
2489-2507
Fox, Keith R.
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Davies, Heather
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Adams, Gill R.
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Portugal, Jose
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Waring, Michael J.
778971c0-a442-4808-ad80-b333f3dc1597
25 March 1988
Fox, Keith R.
9da5debc-4e45-473e-ab8c-550d1104659f
Davies, Heather
c20a0942-d5e1-4afe-8c68-e014204e65dc
Adams, Gill R.
111cc629-b206-45ef-bd6c-07e0a806ff53
Portugal, Jose
03a5b877-a1c2-4125-9897-0fe34426c386
Waring, Michael J.
778971c0-a442-4808-ad80-b333f3dc1597
Fox, Keith R., Davies, Heather, Adams, Gill R., Portugal, Jose and Waring, Michael J.
(1988)
Sequence-specific binding of luzopeptin to DNA.
Nucleic Acids Research, 16 (6), .
(doi:10.1093/nar/16.6.2489).
Abstract
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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Published date: 25 March 1988
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Funding Information: ACKNOWLEDGMENTS This work was supported by grants from the Cancer Research Campaign the Medical Research Council and the Royal Society. Ue thank Mark Freeman and Dean Gentle for technical assistance.
Identifiers
Local EPrints ID: 475572
URI: http://eprints.soton.ac.uk/id/eprint/475572
ISSN: 0305-1048
PURE UUID: 05edbe48-787a-4b04-bedf-5339d010f8e1
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Date deposited: 21 Mar 2023 17:51
Last modified: 18 Mar 2024 02:32
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Author:
Heather Davies
Author:
Gill R. Adams
Author:
Jose Portugal
Author:
Michael J. Waring
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